KR20050117593A - Detection method of genetic recombinant food and detection kit of that - Google Patents

Detection method of genetic recombinant food and detection kit of that Download PDF

Info

Publication number
KR20050117593A
KR20050117593A KR1020000033931A KR20000033931A KR20050117593A KR 20050117593 A KR20050117593 A KR 20050117593A KR 1020000033931 A KR1020000033931 A KR 1020000033931A KR 20000033931 A KR20000033931 A KR 20000033931A KR 20050117593 A KR20050117593 A KR 20050117593A
Authority
KR
South Korea
Prior art keywords
leu
protein
gly
val
ser
Prior art date
Application number
KR1020000033931A
Other languages
Korean (ko)
Inventor
박희영
Original Assignee
박희영
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by 박희영 filed Critical 박희영
Priority to KR1020000033931A priority Critical patent/KR20050117593A/en
Priority to KR1020010035066A priority patent/KR20020000127A/en
Priority to AU2001274652A priority patent/AU2001274652A1/en
Priority to PCT/KR2001/001054 priority patent/WO2001098523A2/en
Publication of KR20050117593A publication Critical patent/KR20050117593A/en

Links

Classifications

    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K16/00Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/16Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from plants
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09Recombinant DNA-technology
    • C12N15/63Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
    • C12N15/79Vectors or expression systems specially adapted for eukaryotic hosts
    • C12N15/82Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
    • C12N15/8241Phenotypically and genetically modified plants via recombinant DNA technology
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/02Food
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53Immunoassay; Biospecific binding assay; Materials therefor
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
    • G01N33/48Biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/68Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
    • G01N33/6803General methods of protein analysis not limited to specific proteins or families of proteins

Landscapes

  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Chemical & Material Sciences (AREA)
  • Molecular Biology (AREA)
  • Genetics & Genomics (AREA)
  • Immunology (AREA)
  • Biomedical Technology (AREA)
  • Physics & Mathematics (AREA)
  • General Health & Medical Sciences (AREA)
  • Biochemistry (AREA)
  • Food Science & Technology (AREA)
  • Biotechnology (AREA)
  • Organic Chemistry (AREA)
  • Medicinal Chemistry (AREA)
  • Urology & Nephrology (AREA)
  • Hematology (AREA)
  • Analytical Chemistry (AREA)
  • Cell Biology (AREA)
  • Pathology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Microbiology (AREA)
  • General Physics & Mathematics (AREA)
  • Biophysics (AREA)
  • Zoology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • General Engineering & Computer Science (AREA)
  • Wood Science & Technology (AREA)
  • Botany (AREA)
  • Plant Pathology (AREA)
  • Bioinformatics & Computational Biology (AREA)
  • Peptides Or Proteins (AREA)
  • Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)

Abstract

본 발명은 유전자재조합 식품의 검사방법과 검사키트에 관한 것으로 유전자재조합 식물에 의해 발현되는 재조합 단백질을 검출하여 유전자변형 여부를 확인하는 검사방법이다. 본 발명은 재조합 단백질에 대한 항체를 제공하여 재조합 식물뿐만 아니라 가공식품에서도 재조합단백질 발현 여부를 쉽게 알 수 있어 유전자변형 식품을 쉽게 선별 할 수 있다.The present invention relates to a test method and test kit of genetically modified foods is a test method for detecting the genetic modification by detecting a recombinant protein expressed by the genetically modified plant. The present invention provides an antibody to the recombinant protein, so that it is easy to know whether the recombinant protein is expressed in the processed food as well as the recombinant plant, so that the genetically modified food can be easily selected.

Description

유전자재조합 식품의 검사방법과 검사키트{Detection method of genetic recombinant food and detection kit of that}Detection method of genetic recombinant food and detection kit of that}

본 발명은 유전자재조합 식품의 검사방법과 검사키트에 관한 것으로서, 더욱 상세하게는 천연형질의 식물에 의해 제조된 식품과 비교하여 유전자재조합 식물에 의해 제조된 식품인지 여부를 검사할 수 있는 검사방법과 검사키트에 관한 것이다.The present invention relates to a test method and a test kit of genetically modified foods, and more particularly, a test method capable of testing whether the food is manufactured by a genetically modified plant as compared to a food produced by a plant of natural form; It is about the inspection kit.

유전자재조합식물(Genetically Modified Organism : GMO)이란 통상적으로 식물의 생산량 증대, 유통, 가공상의 편의를 위하여 유전공학기술로 기존의 번식방법으로는 나타날 수 없는 형질이나 유전자를 지니도록 개발된 식물을 통칭한다. 유전자재조합식물 중 농작물의 유전자 변형은 주로 생산량을 증가시키는 형질, 병충해에 저항적인 형질, 고농도의 농약에 저항적인 형질, 긴 유통기간에도 쉽게 상하지 않는 형질, 식물의 모양이나 빗깔, 맛이 향상된 형질로 이루어지며 앞으로 더욱 다양한 형질을 도입하여 유전자재조합식물을 개발 할 수 있다.Genetically Modified Organism (GMO) is a generic term for plants developed to have traits or genes that cannot be represented by existing breeding methods by genetic engineering techniques for the purpose of increasing plant yield, distribution, and processing convenience. . Genetic modifications of crops in GM plants are mainly those that increase production, resistance to pests, resistance to high concentrations of pesticides, properties that do not easily deteriorate even during long shelf life, and traits that improve plant shape, color, or taste. It is possible to develop genetically modified plants by introducing more diverse traits.

유전자재조합식물의 상업화는 1994년 미국 칼젠(Calgene)사가 잘 물러지지 않는 토마토를 개발한 이후 빠르게 진행되었으며, 1996년 몬산톤사의 대두와 노바티스사의 옥수수가 본격적으로 상품화되었다. 초기 유전자재조합식물 재배는 유전자재조합식물을 개발한 회사가 일반종자 보다 비싸게 판매함에도 불구하고 농민의 입장에서는 농약과 비료의 비용이 크게 줄고 병충해가 감소해 실질적으로 큰 이익을 볼 수 있기 때문에 법적인 규제가 마련되지 못하고 인체에 미칠 파장 또한 예측하지 못한 채 급격하게 증가하여, 1994년부터 1998년까지 FDA의 검증을 마치고 시판이 허용된 유전자재조합식물은 옥수수, 토마토, 감자, 대두 등을 중심으로 39종에 이르며, 6년 이내에 시판될 것으로 예상되는 제품도 30여종에 이른다. The commercialization of genetically modified plants has been rapid since 1994, when Calgene developed a tomato that did not fall well, and in 1996, Monsanton's soybeans and Novartis corn were commercialized. In the early stages of GM plant cultivation, despite the fact that the company that developed the GM plant sold more expensive than the general seed, farmers could benefit substantially from the cost of pesticides and fertilizers and the reduction of pests. Unexpectedly, the wavelengths on the human body have also increased rapidly, with unpredictable effects, and the genetically modified plants, which were approved by the FDA from 1994 to 1998, were allowed to be marketed in 39 species, including corn, tomatoes, potatoes, and soybeans. More than 30 products are expected to be released within six years.

유전자재조합식물은 제초제를 덜 쓰고 적은 노동력과 생산비용으로도 많은 수확량을 올릴 수 있기 때문에 기업과 농민에게 모두 경제적 이득을 주고 전 인류의 식량문제와 환경문제를 해결할 수 있는 잠재력이 있다는 찬성 여론과, 유전자재조합식물의 식품안정성이 검증되지 않았으며, 유전자재조합식물의 장기간 재배로 생태계 교란과 생물 다양성이 파괴되어 궁극적으로 인류에게 해를 준다는 반대여론이 형성되어 있으며, 또한 유전자재조합식물을 나타내는 라벨링 도입 여부도 논란의 대상이 되고 있다. Opinion that genetically modified plants can produce higher yields with less herbicides and less labor and production costs has the potential to provide economic benefits for both businesses and farmers and solve food and environmental problems for all humankind. The food safety of GM plants has not been verified, and there has been a growing consensus that long-term cultivation of GM plants destroys ecosystem disruption and biodiversity and ultimately harms humanity. Also controversial.

현재 우리나라에서는 유전자재조합식품 등의 표시기준이 고시되어 1년간의 유예기간을 거쳐 2001년 7월부터 농수산물품질관리법 제 16조의 규정에 의하여 유전자변형 농수산물임을 표시하여야 하는 원재료를 주요 원재료로 1이상 사용하여 제조, 가공한 식품 또는 식품첨가물은 유전자변형 농수산물임을 표시하는 것으로 입안되었고, 제조나 가공과정중 유전자재조합 DNA 또는 외래 단백질이 제거되어 최종 제품에 유전자재조합 DNA 또는 외래 단백질을 함유하고 있지 않는 유전자재조합 식품 등은 유전자변형 농수산물임을 표시하는 것에 제외되었다. 따라서 유전자재조합 유전자 및 단백질을 검사 할 수 있는 방법들이 체계화 실용화되어야 한다.Currently, in Korea, the labeling standard of genetically modified foods is announced, and after one year grace period, from July 2001, the raw materials that must be labeled as genetically modified agricultural and marine products according to the provisions of Article 16 of the Agricultural Products Quality Management Act Manufactured or processed foods or food additives are designed to indicate that they are genetically modified agricultural and aquatic products, and genetically modified foods that do not contain genetically engineered DNA or foreign protein in the final product due to the removal of the genetically engineered DNA or foreign protein during manufacture or processing And the like are excluded from the indication that they are genetically modified agricultural products. Therefore, methods for testing genetically modified genes and proteins should be systematically implemented.

현재 식물의 유전자조작여부를 확인하기 위하여 개발된 방법은 유전자재조합식물의 DNA를 검출하는 방법과 단백질을 검출하는 두 가지이다. DNA를 검출하는 방법은 대표적으로 Takara의 GMO 검사키트로 유전자재조합식물의 외래 유전자를 증폭시킬 수 있는 특이적 프라이머로 PCR을 수행하여 검사한다. 하지만 검사에 소요되는 시간이 길고, 재현성이 떨어지며 실제 외래단백질의 발현 여부는 확인 할 수 없는 문제점을 가지고 있다. 또한 상기 단백질 검사방법은 미국 SDI사가 EPSPS에 대한 검사키트를 개발하였으나 가공식품에서의 유전자재조합여부를 검사할 수 없으며 또한 통상적인 상기 단백질 검사방법은 종자에 대하여 빠르고 우수한 재현성을 가지나 유전자재조합식물로 제조된 가공식품에서의 외래단백질 검사가 어려운 실정이다. Currently, the methods developed to check whether the plant has been genetically modified include two methods of detecting DNA of GM plants and protein. The DNA detection method is typically performed by PCR using a specific primer capable of amplifying a foreign gene of a recombinant plant by Takara's GMO test kit. However, the test takes a long time, has a low reproducibility, and there is a problem that the actual expression of foreign protein cannot be confirmed. In addition, the protein test method developed by US SDI test kit for EPSPS, but can not test the genetic recombination in the processed food, and the conventional protein test method has a fast and excellent reproducibility for seeds, but is produced as a genetically modified plant It is difficult to test foreign proteins in processed foods.

따라서 유전자재조합식물과 유전자재조합식물로 제조한 식품을 검정하기 위한 새로운 기술이 절실히 요구되고 있는 실정이다.Therefore, there is an urgent need for new technologies for testing GM plants and foods made from GM plants.

따라서, 본 발명은 유전자재조합식품을 검정할 수 있는 방법을 제공하는 것을 목적으로 한다. Accordingly, an object of the present invention is to provide a method for assaying genetically modified foods.

또한 본 발명은 유전자재조합식품을 검정할 수 있는 검사키트를 제공하는 것을 목적으로 한다.It is another object of the present invention to provide a test kit capable of assaying genetically modified foods.

상기의 목적을 달성하기 위하여 본 발명은 유전자재조합식물에 형질전환된 DNA에서 발현되는 재조합단백질의 프로테아제 분해지도(protease cleavage map)를 분석하고, 상기 분해지도에서 분석한 펩타이들 중 동종의 천연식물 단백질의 프로테아제 분해지도로 제조되는 펩타이드와 상동성을 가지지 않는 일련의 펩타이드를 선택하고, 상기의 선택된 펩타이드의 아미노산 서열로 합성펩타이드를 제조하고, 및 상기 합성펩타이드로 항체를 제조하는 것을 특징으로 하는 재조합단백질에 특이적으로 결합하는 항체를 제공한다. In order to achieve the above object, the present invention analyzes the protease cleavage map of the recombinant protein expressed in the DNA transformed into the genetically modified plant, the same natural plant of the peptides analyzed in the degradation map Recombination characterized in that a series of peptides having no homology with the peptide produced by the protease digestion map of the protein is selected, a synthetic peptide is prepared from the amino acid sequence of the selected peptide, and the antibody is prepared from the synthetic peptide. Provided are antibodies that specifically bind to proteins.

또한 본 발명은 상기의 재조합단백질에 특이적으로 결합하는 항체를 식품에 반응시켜 항원항체반응여부를 확인함으로써 천연식물로 제조한 식품과 유전자재조합식품을 식별하는 것을 특징으로 하는 유전자재조합식품 검사방법을 제공한다.In another aspect, the present invention is a genetic recombinant food test method characterized in that to identify the food and genetically modified foods produced by natural plants by reacting the antibody specifically binding to the recombinant protein to food to determine whether the antigen antibody reaction to provide.

또한 본 발명은 검사대상 식품으로부터 단백질을 추출한 단백질추출액, 상기 단백질추출액 중의 단백질을 분해하는 효소를 함유하는 효소반응액, 상기 효소에 의하여 분해된 단백질 중의 재조합단백질과 결합할 수 있는 상기 제 1항의 항체, 상기 항체가 표면의 소정부분에 묻혀 있는 스트립, 상기 항체가 재조합단백질과 결합할 때 이를 표시할 수 있는 발색단이 연결된 발색항체, 및 상기 효소에 의한 단백질 분해가 일어나는 반응기를 포함하는 것을 특징으로 하는 유전자재조합식품 검사키트를 제공한다.In another aspect, the present invention is a protein extract extracted from the food to be tested, an enzyme reaction solution containing an enzyme that breaks down the protein in the protein extract, the antibody of claim 1 capable of binding to the recombinant protein in the protein degraded by the enzyme A chromophoric antibody linked to a chromophore that can display the antibody when the antibody binds to a recombinant protein, and a reactor in which proteolysis by the enzyme occurs. Provide genetically modified food test kits.

본 발명은 검사대상 식품으로부터 단백질을 추출한 단백질추출액, 상기 단백질추출액 중의 단백질을 분해하는 효소를 함유하는 효소반응액, 상기 효소에 의하여 분해된 단백질 중의 재조합단백질과 결합할 수 있는 상기 제 1항의 항체, 상기 항체가 표면에 코팅되어 있는 10-웰 플레이트, 상기 항체가 재조합단백질과 결합할 때 이를 표시할 수 있는 발색단이 연결된 발색항체, 및 상기 효소에 의한 단백질 분해가 일어나는 반응기를 포함하는 것을 특징으로 하는 유전자재조합식품 검사키트를 제공한다.The present invention is a protein extract extracted from the food to be tested, an enzyme reaction solution containing an enzyme that breaks down the protein in the protein extract, the antibody of claim 1 capable of binding to the recombinant protein in the protein degraded by the enzyme, A 10-well plate coated with the antibody on the surface, a chromophoric antibody linked to a chromophore capable of indicating when the antibody binds to a recombinant protein, and a reactor in which proteolysis by the enzyme occurs Provide genetically modified food test kits.

이하 본 발명을 상세하게 설명한다.Hereinafter, the present invention will be described in detail.

본 발명의 유전자재조합식품의 검사방법은 재조합식물에서 발현되는 재조합단백질에 대한 항체를 만들어 식품에 항체반응을 시킴으로써 유전자조작여부를 확인하는 것이다. The test method for genetically engineered foods of the present invention is to make an antibody against a recombinant protein expressed in a recombinant plant and to confirm genetic manipulation by subjecting the food to an antibody reaction.

본 발명의 상기 재조합단백질은 통상적으로 농작물에 형질전환시키는 유전자에 의한 재조합단백질로 제초제에 저항성을 나타내는 형질, 병충해에 저항성을 나타내는 형질, 냉해에 저항성을 나타내는 형질, 저장성을 향상시키는 형질, 및 생산력을 향상시키는 형질을 포함하는 것이 바람직하며 또한 유전자재조합식물에서 발현되는 재조합 단백질들이 바람직하다.The recombinant protein of the present invention is a recombinant protein by a gene that is usually transformed into crops, traits resistant to herbicides, traits resistant to pests, traits resistant to cold and cold, traits that improve shelf life, and productivity. It is preferred to include the trait to be enhanced and also recombinant proteins expressed in genetically modified plants.

본 발명에서는 EPSPS, PAT 및 BT 재조합단백질을 검출할 수 있는 검사방법을 실험하였다.In the present invention, the test method for detecting the EPSPS, PAT and BT recombinant protein was tested.

상기 EPSPS는 5-에놀피루빌쉬키마트-3-포스페이트 신테이즈(enolpyru vylshikimate-3-phosphate synthase)단백질로 글리포세이트(glyphosate)라는 제초능을 가지는 화학물질에 내성을 갖는 형질을 나타낸다. 글리포세이트는 전세계에서 가장 많이 판매되는 라운드업(round-up)제초제의 핵심성분으로 우리나라에서도 근사미라는 제초제로 시판되고 있다. 이러한 글리포세이트에 저항성을 가지는 재조합식물로 몬산토사의 글리포세이트 내성/해충 내성 옥수수(Agrobacterium sp.종 CP4 EPSPS유전자와 글리포세이트 내성종 중 Ochrobactrum anthropi의 glyphosate oxidaoreductase유전자), 글리포세이트 내성 면실(Agrobactarium spp. CP4 EPSPS유전자), 및 글리포세이트 내성 캐놀라(Agrobactarium spp. CP4 EPSPS유전자)가 개발되어 시판되고 있다. The EPSPS is a 5-enolpyrubilishkimat-3-phosphate synthase (enolpyru vylshikimate-3-phosphate synthase) protein that represents a trait that is resistant to a chemical having a herbicidal ability (glyphosate). Glyphosate is a key ingredient in the world's best-selling round-up herbicide and is marketed as a herbicide in Korea. These glyphosate-resistant recombinant plants include glyphosate oxidaoreductase gene from Monsanto's glyphosate resistant / pest resistant corn (Agrobacterium sp. Species CP4 EPSPS gene and glyphosate oxidaoreductase gene of Ochrobactrum anthropi among glyphosate resistant species) Agrobactarium spp.CP4 EPSPS gene), and glyphosate resistant canola (Agrobactarium spp. CP4 EPSPS gene) have been developed and marketed.

상기 PAT는 스트렙토마이스 비리도크로모진(Streptomyces viridoch romogenes)의 포스피노트리신 아세틸트랜스퍼레이즈(Phosphinothricin acetyl transferase)유전자와 스트렙토마이세스 하이그로스코피커스(Streptomy ces hygroscopicus)의 포스피노트리신 아세틸 하이드롤레이즈(Phosphino thricin acetyl hydrolase)유전자로 제초제 글리포세이트에 저항성을 가지는 유전자이다. 상기 PAT로 제조된 재조합식물은 데칼브 제네틱스 사(Dekalb Genetics Corp)의 글리포세이트 내성 옥수수(Streptomyces hygro scopicus의 Phosphinothricin acetyl hydrolase유전자), 아게보사(Agevo Inc)의 글루포시네이트 내성 캐놀라(Steptomyces virdochromogenes의 Phosphinothricin acetyl transferase)와 글루포시네이트 내성 옥수수 (Steptomyces virdochromogenes의 Phosphinothricin acetyl transferase) 가 있으며 현재 농업 진흥청에서 PAT로 형질전환된 벼를 개발하였다.The PAT is a phosphinothricin acetyl hydrase of Streptomy ces hygroscopicus and a phosphinothricin acetyl transferase gene of Streptomyces viridoch romogenes . Phosphino thricin acetyl hydrolase) is a gene that is resistant to herbicide glyphosate. Recombinant plants prepared with PAT are glyphosate resistant corn from Dekalb Genetics Corp, Phosphinothricin acetyl hydrolase gene from Streptomyces hygro scopicus, and glufosinate resistant canola from Agevo Inc. of Steptomyces virdochromogenes. Phosphinothricin acetyl transferase and glufosinate-resistant corn (Phosphynotnotincin acetyl transferase from Steptomyces virdochromogenes) are currently developed by PDA-developed rice.

상기 BT는 바실러스 투린지엔시스(Bacillus thuringiensis)의 cryIA과 cryIII A 유전자를 식물에 형질전화하여 해충에 내성을 가지게 한다. BT 작물로는 몬산토사의 해충 내성 옥수수(crylA(b)유전자), 해충 내성 옥수수(crylA(b)유전자), 및 해충 내성 감자(crylll A유전자), 노트럽 킹사(Northrup King)의 해충 내성 옥수수(crylA(b)유전자), 시바-게이지사(Ciba-Geigy Corp)의 해충 내성 옥수수(crylA(b)유전자) 등이 있으며 현재 유전자재조합 옥수수로 유통되고 있을 뿐만 아니라 국내로 수입되고 있다.The BT transforms the cryIA and cryIII A genes of Bacillus thuringiensis into plants to make them resistant to pests. BT crops include Monsanto's pest-resistant maize (crylA (b) gene), pest-resistant maize (crylA (b) gene), and pest-resistant maize (crylll A) and pest-resistant maize (Northrup King) crylA (b) gene, pesticide-tolerant corn (CrylA (b) gene) of Ciba-Geigy Corp, and the like are currently being distributed as genetically modified corn as well as imported into Korea.

본 발명은 식물에 형질도입된 유전자의 단백질 서열을 분석하고 재조합단백질이 여러 종류의 프로테아제로 잘렸을 때 생성되는 펩타이드가 다른 여타의 단백질들이 동일 프로테아제에 의해 잘렸을 때 생기는 펩타이드와 아미노산 서열상 구별되는 특정 펩타이드를 선택한다.The present invention analyzes the protein sequence of genes transduced in plants, and the peptide produced when the recombinant protein is cut by several proteases is distinguished from the peptide and amino acid sequence produced when other proteins are cut by the same protease. Select a specific peptide.

상기 프로테아제는 트립신(trysin), 키모트립신(chymotrypsin), 펩신, 섭맥실라루스 프로테이즈(submaxillarus protease), 및 St. 아우레우스 V8 프로테이즈(St. aureus V8 protease)로 이루어지는 군으로부터 한가지 이상 선택하는 것이 바람직하며, 상기 프로테아제에 의해 생기는 펩타이드들 중 상기 특정 펩타이드는 10개 이상의 아미노산으로 이루어지는 펩타이드가 바람직하다. 상기 트립신은 단백질의 알지닌(R), 라이신(K) 잔기의 카르복시 말단을 분해하고 키모트립신은 단백질의 페닐알라닌(F), 타이로신(Y), 트립토판(W) 잔기의 카르복시 말단을, 섭맥실라루스 프로테이즈는 단백질의 알지닌(R)잔기의 카르복시 말단을, St. 아우레우스 V8 프로테이즈는 단백질의 아스파르트산(D), 글루탐산(E) 잔기의 카르복시 말단을 분해한다.상기에서 선택한 다른 단백질과의 상동성이 희박한 특정 펩타이들에 대한 합성펩타이드를 합성하고 다시 합성 펩타이드에 대한 항체들을 제조한다.The protease is trysin, chymotrypsin, pepsin, submaxillarus protease, and St. It is preferable to select one or more from the group consisting of Aureus V8 protease, and among the peptides produced by the protease, the specific peptide is preferably a peptide consisting of 10 or more amino acids. The trypsin decomposes the carboxy terminus of the alginine (R) and lysine (K) residues of the protein, and the chymotrypsin represents the carboxy terminus of the phenylalanine (F), tyrosine (Y) and tryptophan (W) residues of the protein, Protease refers to the carboxy terminus of the alginine (R) residue of the protein. Aureus V8 Protease decomposes the carboxy terminus of the aspartic acid (D) and glutamic acid (E) residues of a protein.Synthetic peptides are synthesized for specific peptides that have little homology with other proteins selected above. Again antibodies to synthetic peptides are prepared.

본 발명의 선택된 특정 펩타이드를 하기에 나타내었다. Certain selected peptides of the invention are shown below.

EPSPS에서 선택한 펩타이드는 염기서열작성프로그램으로 작성하여 각각에 서열번호를 지정하였고, 펩타이드 서열은 하기 표 1에 나타내었다.Peptides selected from the EPSPS was created by the nucleotide sequencer program, and assigned the sequence number to each, peptide sequences are shown in Table 1 below.

프로테아제Protease 선택한 특정펩타이드Selected specific peptide 서열번호SEQ ID NO: 트립신Trypsin EGDTWIIDGVGNGGLLAPEAPLDFGNAATGCEGDTWIIDGVGNGGLLAPEAPLDFGNAATGC 1One LTGQVIDVPGDPSSTAFPLVAALLVPGSDVTILNVLMNPTLTGQVIDVPGDPSSTAFPLVAALLVPGSDVTILNVLMNPT 22 APSMIDEYPILAVAAAFAEGATVMNGLEELAPSMIDEYPILAVAAAFAEGATVMNGLEEL 33 IAMSFLVMGLVSENPVTVDDATMIATSFPEFMDLMAGLGAIAMSFLVMGLVSENPVTVDDATMIATSFPEFMDLMAGLGA 44 키모트립신Chymotrypsin GGLASGETRITGLLEGEDVINTGKAMQAMGARIRKEGDTGGLASGETRITGLLEGEDVINTGKAMQAMGARIRKEGDT 55 IGDASLTKRPMGRVLNPLREMGVQVKSEHGDRLPVTLRGPKTPTPIIGDASLTKRPMGRVLNPLREMGVQVKSEHGDRLPVTLRGPKTPTPI 66 VPMASAQVKSAVLLAGLNTPGITTVIEPIMTRDHTEKMLQGVPMASAQVKSAVLLAGLNTPGITTVIEPIMTRDHTEKMLQG 77 GANLTVETDADGVRTIRLEGRGKLTGQVIDVPGDPSSTAGANLTVETDADGVRTIRLEGRGKLTGQVIDVPGDPSSTA 88 LVPGSDVTILNVLMNPTRTGLILTLQEMGADIEVINPRLAGGEDVADLRVRSSTLKGVTVPEDRAPSMIDELVPGSDVTILNVLMNPTRTGLILTLQEMGADIEVINPRLAGGEDVADLRVRSSTLKGVTVPEDRAPSMIDE 99 AEGATVMNGLEELRVKESDRLSAVANGLKLNGVDCDEGETSLVVRGRPDGKGLGNASGAAVATHLDHRIAMSAEGATVMNGLEELRVKESDRLSAVANGLKLNGVDCDEGETSLVVRGRPDGKGLGNASGAAVATHLDHRIAMS 1010 섭맥실라루스Supmacilarus KEGDTWIIDGVGNGGLLAPEAPLDFGNAATGCKEGDTWIIDGVGNGGLLAPEAPLDFGNAATGC 1111 VPMASAQVKSAVLLAGLNTPGITTVIEPIMTVPMASAQVKSAVLLAGLNTPGITTVIEPIMT 1212 GKLTGQVIDVPGDPSSTAFPLVAALLVPGSDVTILNVLMNPTGKLTGQVIDVPGDPSSTAFPLVAALLVPGSDVTILNVLMNPT 1313 APSMIDEYPILAVAAAFAEGATVMNGLEELAPSMIDEYPILAVAAAFAEGATVMNGLEEL 1414 LSAVANGLKLNGVDCDEGETSLVVLSAVANGLKLNGVDCDEGETSLVV 1515 IAMSFLVMGLVSENPVTVDDATMIATSFPEFMDLMAGLGAKIELSDTKAAIAMSFLVMGLVSENPVTVDDATMIATSFPEFMDLMAGLGAKIELSDTKAA 1616 St. 아우레우스 V8St. Aureus V8 MSHGASSRPATARKSSGLSGTVRIPGMSHGASSRPATARKSSGLSGTVRIPG 1717 VINTGKAMQAMGARIRKVINTGKAMQAMGARIRK 1818 FGNAATGCRLTMGLVGVYFGNAATGCRLTMGLVGVY 1919 RLPVTLRGPKTPTPITYRVPMASAQVKSAVLLAGLNTPGITTVIRLPVTLRGPKTPTPITYRVPMASAQVKSAVLLAGLNTPGITTVI 2020 VTILNVLMNPTRTGLILTLQVTILNVLMNPTRTGLILTLQ 2121 트립신+키모트립신Trypsin + chymotrypsin IIDGVGNGGLLAPEAPLDIIDGVGNGGLLAPEAPLD 2222 SAVLLAGLNTPGITTVIEPIMTSAVLLAGLNTPGITTVIEPIMT 2323 PLVAALLVPGSDVTILNVLMNPTPLVAALLVPGSDVTILNVLMNPT 2424 TGLILTLQEMGADIEVINPTGLILTLQEMGADIEVINP 2525 GLGNASGAAVATHLDHGLGNASGAAVATHLDH 2626 LVMGLVSENPVTVDDATMIATSLVMGLVSENPVTVDDATMIATS 2727

PAT는 스트렙토마이스 비리도크로모진(Streptomyces viridoch romogenes)의 포스피노트리신 아세틸트랜스퍼레이즈(Phosphinothricin ace tyl transferase)유전자를 PAT1으로, 스트렙토마이세스 하이그로스코피커스(Streptomy ces hygroscopicus)의 유전자를 PAT2로 하였다. 각각의 선택한 펩타이드는 염기서열작성프로그램으로 작성하여 각각에 서열번호를 지정하였고, 펩타이드 서열은 하기 표 2로 나타내었다.PAT is the PAT1 gene for the phosphinothricin acetyltransase gene of Streptomyces viridoch romogenes and PAT2 for the gene of Streptomy ces hygroscopicus . . Each selected peptide was prepared by a nucleotide sequencing program, each assigned a sequence number, and peptide sequences are shown in Table 2 below.

처리한 프로테아제Treated Protease 선택한 특정펩타이드 서열Selected Specific Peptide Sequence 서열번호SEQ ID NO: PAT1(스트렙토마이스 비리도크로모진) PAT1 (streptomyces viridochromine) 트립신 Trypsin PATAADMAAVCDIVNHYIETSTVNFPATAADMAAVCDIVNHYIETSTVNF 2828 TEPQTPQEWIDDLETEPQTPQEWIDDLE 2929 YPWLVAEVEGVVAGIAYAGPWYPWLVAEVEGVVAGIAYAGPW 3030 키모트립신Chymotrypsin VSHRHQRLGLGSTLVSHRHQRLGLGSTL 3131 KSVVAVIGLPNDPSVRLHEALGKSVVAVIGLPNDPSVRLHEALG 3232 St. 아우레우스 V8 St. Aureus V8 GVVAGIAYAGPWKARNAYGVVAGIAYAGPWKARNAY 3333 STVYVSHRHQRLGLGSTLYTHLLKSMSTVYVSHRHQRLGLGSTLYTHLLKSM 3434 ALGYTARGTLRAAGYKHGGWHALGYTARGTLRAAGYKHGGWH 3535 섭맥실라루스 Supmacilarus PATAADMAAVCDIVNHYIETSTVNFPATAADMAAVCDIVNHYIETSTVNF 3636 YPWLVAEVEGVVAGIAYAGPWKAYPWLVAEVEGVVAGIAYAGPWKA 3737 TLYTHLLKSMEAQGFKSVVAVIGLPNDPSVTLYTHLLKSMEAQGFKSVVAVIGLPNDPSV 3838 트립신+키모트립신 Trypsin + chymotrypsin PATAADMAAVCDIVNHPATAADMAAVCDIVNH 3939 LVAEVEGVVAGIALVAEVEGVVAGIA 4040 SVVAVIGLPNDPSVSVVAVIGLPNDPSV 4141 PAT2(스트렙토마이세스 하이그로스코피커스) PAT2 (Streptomyces hygroscopic picus) 트립신 Trypsin ATEADMPAVCTIVNHYIETSTVNFATEADMPAVCTIVNHYIETSTVNF 4242 YPWLVAEVDGEVAGIAYAGPWYPWLVAEVDGEVAGIAYAGPW 4343 HGNWHDV GFWQIDFSLPVPPHGNWHDV GFWQIDFSLPVPP 4444 키모트립신Chymotrypsin MSPERRPADIRRATEADMPAVCTIVNHMSPERRPADIRRATEADMPAVCTIVNH 4545 SVVAVIGLPNDPSVRMHEALGSVVAVIGLPNDPSVRMHEALG 4646 St. 아우레우스 V8St. Aureus V8 STVYVSPRHQRTGLGSTLYTHLLKSLSTVYVSPRHQRTGLGSTLYTHLLKSL 4747 ALGYAPRGMLRAAGFKHGNWHALGYAPRGMLRAAGFKHGNWH 4848 트립신+키모트립신Trypsin + chymotrypsin ATEADMPAVCTIVNHATEADMPAVCTIVNH 4949 SVVAVIGLPNDPSVSVVAVIGLPNDPSV 5050

BT는 MonBT 유전자, Cry1 유전자, CryB1 유전자, CryHD-1 유전자, CryIII 유전자에서 선택한 각각의 펩타이드를 염기서열작성프로그램으로 작성하여 각각에 서열번호를 지정하였고, 펩타이드 서열은 하기 표 3에 나타내었다.  BT prepared each peptide selected from MonBT gene, Cry1 gene, CryB1 gene, CryHD-1 gene, CryIII gene by sequencing program and assigned the sequence number to each, and peptide sequences are shown in Table 3 below.

유전자gene 프로테아제Protease 선택된 특정펩타이드 서열 Selected Specific Peptide Sequence 서열번호SEQ ID NO: BT-1(MonBT)BT-1 (MonBT) 트립신 Trypsin IQFNDMNSALTTAIPLFAVQNYQVPLLSVYVQAANLHLSVLIQFNDMNSALTTAIPLFAVQNYQVPLLSVYVQAANLHLSVL 5151 GEYYWSGHQIMASPVGFSGSNQIGLGEYYWSGHQIMASPVGFSGSNQIGL 5252 TDVTDYHIDQVSNLVECLSDEFCLDETDVTDYHIDQVSNLVECLSDEFCLDE 5353 CAHHSHHFSLDIDVGCTDLNEDLGVWVIFCAHHSHHFSLDIDVGCTDLNEDLGVWVIF 5454 키모트립신 Chymotrypsin RGSAQGIEGSIRSPHLMDILNSITIRGSAQGIEGSIRSPHLMDILNSITI 5555 CLDEKKELSEKVKHAKRLSDERNLLQDPNCLDEKKELSEKVKHAKRLSDERNLLQDPN 5656 LEGRAPLVGEALARGQEGLEGRAPLVGEALARGQEG 5757 섭맥실라루스 Supmacilarus ELTLTVLDIVSLFPNYDSPPYPIELTLTVLDIVSLFPNYDSPPYPI 5858 GEYYWSGHQIMASPVGFSGSNQIGLKTDVTDYHIDQVSNLVECLSDEFCLDEKKELSEKVKHAKGEYYWSGHQIMASPVGFSGSNQIGLKTDVTDYHIDQVSNLVECLSDEFCLDEKKELSEKVKHAK 5959 GSTDITIQGGDDVFKENYVTLLGTFDECYPTYLYQKIDESKLKAYGSTDITIQGGDDVFKENYVTLLGTFDECYPTYLYQKIDESKLKAY 6060 YNAKHETVNVPGTGSLWPLSAPSPIGKCAHHSHHFSLDIDVGCTDLNEDLGVWVIFKIKTQDGHEYNAKHETVNVPGTGSLWPLSAPSPIGKCAHHSHHFSLDIDVGCTDLNEDLGVWVIFKIKTQDGHE 6161 St. 아우레우스 V8St. Aureus V8 MNSALTTAIPLFAVQNYQVPLLSVYVQAANLHLSVLRMNSALTTAIPLFAVQNYQVPLLSVYVQAANLHLSVLR 6262 TVNVPGTGSLWPLSAPSPIGKCAHHSHHFSLTVNVPGTGSLWPLSAPSPIGKCAHHSHHFSL 6363 트립신+ 키모트립신 Trypsin + Chymotrypsin NDMNSALTTAIPLNDMNSALTTAIPL 6464 HIDQVSNLVECLSHIDQVSNLVECLS 6565 GSTDITIQGGDDVGSTDITIQGGDDV 6666 SLDIDVGCTDLNEDLGVSLDIDVGCTDLNEDLGV 6767 BT-2BT-2 트립신 Trypsin IETGYTPIDISLSLTQFLLSEFVPGAGFVLGLVDIIWGIFGPSQWDAFLVQIEQLINQIETGYTPIDISLSLTQFLLSEFVPGAGFVLGLVDIIWGIFGPSQWDAFLVQIEQLINQ 6868 GFNYWSGHQITTSPVGFSGPEFAFPLFGNAGNAAPPVLVSLTGLGIFGFNYWSGHQITTSPVGFSGPEFAFPLFGNAGNAAPPVLVSLTGLGIF 6969 IILGSGPNNQELFVLDGTEFSFASLTTNLPSTIYIILGSGPNNQELFVLDGTEFSFASLTTNLPSTIY 7070 TVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYIDTVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYID 7171 TDGTDYHIDQVSNLVECLSDEFCLDETDGTDYHIDQVSNLVECLSDEFCLDE 7272 CAHHSHHFSLDIDVGCTDLNEDLGVWVIFCAHHSHHFSLDIDVGCTDLNEDLGVWVIF 7373 ESVDALFVNSQYDQLQADTNIAMIHAADESVDALFVNSQYDQLQADTNIAMIHAAD 7474 EAYLPELSVIPGVNAAIFEELEGEAYLPELSVIPGVNAAIFEELEG 7575 FSNCVEEEIYPNNTVTCNDYTVNQEEYGGAYTS FSNCVEEEIYPNNTVTCNDYTVNQEEYGGAYTS 7676 키모트립신Chymotrypsin GNAGNAAPPVLVSLTGLGI GNAGNAAPPVLVSLTGLGI 7777 RQRGTVDSLDVIPPQDNSVPPRAG RQRGTVDSLDVIPPQDNSVPPRAG 7878 QIPLTKSTNLGSGTSVVKGPG QIPLTKSTNLGSGTSVVKGPG 7979 TGGDILRRTSPGLISTLRVNITAPLSQR TGGDILRRTSPGLISTLRVNITAPLSQR 8080 HIDQVSNLVECLSDE HIDQVSNLVECLSDE 8181 CLDEKQELSEKVKHAKRLSDERNLLQDPN CLDEKQELSEKVKHAKRLSDERNLLQDPN 8282 PVSAPKPIGKCGEPNRCAPHLE PVSAPKPIGKCGEPNRCAPHLE 8383 NPDLDCSCRDGEKCAHHSHH NPDLDCSCRDGEKCAHHSHH 8484

BT-2BT-2 키모트립신Chymotrypsin SLDIDVGCTDLNEDLGVSLDIDVGCTDLNEDLGV 8585 DQLQADTNIAMIHAADDQLQADTNIAMIHAAD 8686 GEGCVTIHEIENNTDELGEGCVTIHEIENNTDEL 8787 트립신+키모트립신Trypsin + chymotrypsin GNAGNAAPPVLVSLTGLGIGNAGNAAPPVLVSLTGLGI 8888 GTVDSLDVIPPQDNSVPPGTVDSLDVIPPQDNSVPP 8989 HIDQVSNLVECLSDEHIDQVSNLVECLSDE 9090 SLDIDVGCTDLNEDLGVSLDIDVGCTDLNEDLGV 9191 DQLQADTNIAMIHAADDQLQADTNIAMIHAAD 9292 GEGCVTIHEIENNTDELGEGCVTIHEIENNTDEL 9393 BT-3(Cry-BI)BT-3 (Cry-BI) 트립신Trypsin TDHSLYVAPVVGTVSSFLLTDHSLYVAPVVGTVSSFLL 9494 EFNQQVDNFLNPTQNPVPLSITSSVNTMQQLFLEFNQQVDNFLNPTQNPVPLSITSSVNTMQQLFL 9595 LPQFQIQGYQLLLLPLFAQAANMHLSFILPQFQIQGYQLLLLPLFAQAANMHLSFI 9696 YQSLMVSSGANLYASGSGPQQTQSFTAQNWPFLYSLFQVNSNYILSG ISGTYQSLMVSSGANLYASGSGPQQTQSFTAQNWPFLYSLFQVNSNYILSG ISGT 9797 VNYSGGVSSGLIGATNLNHNFNCSTVLPPLSTPFVVNYSGGVSSGLIGATNLNHNFNCSTVLPPLSTPFV 9898 NNIYAANENGTMIHLAPEDYTGFTISPIHATQVNNQTNNIYAANENGTMIHLAPEDYTGFTISPIHATQVNNQT 9999 VTINGRVYTVSNVNTTTNNDGVNDNGAVTINGRVYTVSNVNTTTNNDGVNDNGA 100100 FSDINIGNIVASDNTNVTLDINVTLNSGTPFDLMNIMFVPTNLPPLYFSDINIGNIVASDNTNVTLDINVTLNSGTPFDLMNIMFVPTNLPPLY 101101 트립신+키모트립신Trypsin + chymotrypsin LNPTQNPVPLSITSSVNTMQQLLNPTQNPVPLSITSSVNTMQQL 102102 PNIGGLPGSTTTHSLNSAPNIGGLPGSTTTHSLNSA 103103 TVSNVNTTTNNDGVNDNGATVSNVNTTTNNDGVNDNGA 104104 SDINIGNIVASDNTNVTLDINVTLNSGTPSDINIGNIVASDNTNVTLDINVTLNSGTP 105105 BT-4(CryHD-1)BT-4 (CryHD-1) 트립신Trypsin IETGYTPIDISLSLTQFLLSEFVPGAGFVLGLVDIIWGIFGPSQWDAFLVQIEQLINQIETGYTPIDISLSLTQFLLSEFVPGAGFVLGLVDIIWGIFGPSQWDAFLVQIEQLINQ 106106 IQFNDMNSALTTAIPLFAVQNYQVPLLSVYVQAANLHLSVLIQFNDMNSALTTAIPLFAVQNYQVPLLSVYVQAANLHLSVL 107107 PFNIGINNQQLSVLDGTEFAYGTSSNLPSAVYPFNIGINNQQLSVLDGTEFAYGTSSNLPSAVY 108108 SGTVDSLDEIPPQNNNVPPSGTVDSLDEIPPQNNNVPP 109109 TVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYIDTVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYID 110110 TDVTDYHIDQVSNLVECLSDEFCLDETDVTDYHIDQVSNLVECLSDEFCLDE 111111 SHHFSLDIDVGCTDLNEDLGVWVIFSHHFSLDIDVGCTDLNEDLGVWVIF 112112 EAYLPELSVIPGVNAAIFEELEGEAYLPELSVIPGVNAAIFEELEG 113113 SNCVEEEVYPNNTVTCNDYTATQEEYEGTYTSSNCVEEEVYPNNTVTCNDYTATQEEYEGTYTS 114114 키모트립신Chymotrypsin RGSAQGIEGSIRSPHLMDILNSITIRGSAQGIEGSIRSPHLMDILNSITI 115115 GTMGNAAPQQRIVAQLGQGVGTMGNAAPQQRIVAQLGQGV 116116 RKSGTVDSLDEIPPQNNNVPPRQGRKSGTVDSLDEIPPQNNNVPPRQG 117117 NNIIPSSQITQIPLTKSTNLGSGTSVVKGPG NNIIPSSQITQIPLTKSTNLGSGTSVVKGPG 118118 GGDILRRTSPGQISTLRVNITAPLSQR GGDILRRTSPGQISTLRVNITAPLSQR 119119 CLDEKKELSEKVKHAKRLSDERNLLQDPN CLDEKKELSEKVKHAKRLSDERNLLQDPN 120120 DRLQADTNIAMIHAADKRVHSIR DRLQADTNIAMIHAADKRVHSIR 121121 NVKGHVDVEEQNNHRSVLVVPE NVKGHVDVEEQNNHRSVLVVPE 122122 트립신+키모트립신Trypsin + chymotrypsin NIGINNQQLSVLDGTE NIGINNQQLSVLDGTE 123123 SGTVDSLDEIPPQNNNVPP SGTVDSLDEIPPQNNNVPP 124124 SATMSSGSNLQSGS SATMSSGSNLQSGS 125125 HIDQVSNLVECLSDE HIDQVSNLVECLSDE 126126 SLDIDVGCTDLNEDLGVSLDIDVGCTDLNEDLGV 127127

BT-4BT-4 GEGCVTIHEIENNTDEL GEGCVTIHEIENNTDEL 128128 BT-5(CryIIIA)BT-5 (CryIIIA) 트립신Trypsin GISVVGDLLGVVGFPFGGALVSFYTNFLNTIWPSEDPWGISVVGDLLGVVGFPFGGALVSFYTNFLNTIWPSEDPW 129129 ALAELQGLQNNVEDYVSALSSALAELQGLQNNVEDYVSALSS 130130 NSMPSFAISGYEVLFLTTYAQAANTHLFLNSMPSFAISGYEVLFLTTYAQAANTHLFL 131131 FQPGYYGNDSFNYWSGNYVSTFQPGYYGNDSFNYWSGNYVST 132132 VEFSQYNDQTDEASTQTYDSVEFSQYNDQTDEASTQTYDS 133133 NVGAVSWDSIDQLPPETTDEPLENVGAVSWDSIDQLPPETTDEPLE 134134 FTGGDIIQCTENGSAATIYVTPDVSYSQFTGGDIIQCTENGSAATIYVTPDVSYSQ 135135 IHYASTSQITFTLSLDGAPFNQYYFDIHYASTSQITFTLSLDGAPFNQYYFD 136136 GDTLTYNSFNLASFSTPFELSGNNLQIGVTGLSAGDGDTLTYNSFNLASFSTPFELSGNNLQIGVTGLSAGD 137137 키모트립신Chymotrypsin AKNKALAELQGLQNNVEDAKNKALAELQGLQNNVED 138138 QKNPVSSRNPHSQGRIRELQKNPVSSRNPHSQGRIREL 139139 DSIDQLPPETTDEPLEKGDSIDQLPPETTDEPLEKG 140140 ELSGNNLQIGVTGLSAGDKVELSGNNLQIGVTGLSAGDKV 141141 섭맥실라루스Supmacilarus LLGVVGFPFGGALVSFYTNFLNTIWPSELLGVVGFPFGGALVSFYTNFLNTIWPSE 142142 YVSALSSWQKNPVSSRNPHSQGRIRELFSQAESHFRNSMPSFAISGYEVLFLTTYAQAANTHLFLLKYVSALSSWQKNPVSSRNPHSQGRIRELFSQAESHFRNSMPSFAISGYEVLFLTTYAQAANTHLFLLK 143143 IITSPFYGNKSSEPVQNLEFNGEKVYRAVANTNLAVWPSAVYSGVTKVEFSQYNIITSPFYGNKSSEPVQNLEFNGEKVYRAVANTNLAVWPSAVYSGVTKVEFSQYN 144144 EPLEKGYSHQLNYVMCFLMQGSRGTIPVLTWTHKSVEPLEKGYSHQLNYVMCFLMQGSRGTIPVLTWTHKSV 145145 SKKITQLPLVKAYKLQSGASVVAGPRFTGGSKKITQLPLVKAYKLQSGASVVAGPRFTGG 146146 VSYSQKYRARIHYASTSQITFTLSLVSYSQKYRARIHYASTSQITFTLSL 147147 TLTYNSFNLASFSTPFELSGNNLQIGVTGLSAGTLTYNSFNLASFSTPFELSGNNLQIGVTGLSAG 148148 St. 아우레우스 V8St. Aureus V8 LLGVVGFPFGGALVSFYTNFLNTIWPSLLGVVGFPFGGALVSFYTNFLNTIWPS 149149 YVSALSSWQKNPVSSRNPHSQGRIRYVSALSSWQKNPVSSRNPHSQGRIR 150150 VLFLTTYAQAANTHLFLLKVLFLTTYAQAANTHLFLLK 151151 KGYSHQLNYVMCFLMQGSRGTIPVLTWTHKSKGYSHQLNYVMCFLMQGSRGTIPVLTWTHKS 152152 SKKITQLPLVKAYKLQSGASVVAGPRFTGGSKKITQLPLVKAYKLQSGASVVAGPRFTGG 153153 트립신+키모트립신Trypsin + chymotrypsin TGGDIIQCTENGSAATITGGDIIQCTENGSAATI 154154 ELSGNNLQIGVTGLSAGDELSGNNLQIGVTGLSAGD 155155

본 발명의 유전자재조합 단백질에 대하여 상기에서 선택한 펩타이들에 대한 항체들은 검사하고자 하는 식품이나 가공식품에 가하여 항원항체반응의 반응성을 검사한다. 검사시 사용하는 항체는 제조한 항체들 중 하나 이상을 선택하여 사용함으로써 검사의 신뢰성을 높일 수 있다. Antibodies to the peptides selected above for the recombinant protein of the present invention is added to the food or processed food to be tested to test the reactivity of the antigen antibody response. The antibody used for the test can increase the reliability of the test by selecting and using one or more of the prepared antibodies.

또한 본 발명의 유전자재조합 단백질의 항원항체반응의 확인은 통상적으로 실험실에서 실시하는 방법으로 수행할 수 있으며 본 발명에서는 항원에 항체가 결합한 것에만 다시 결합하는 비활성상태의 형광단백질이 연결된 2차 항체를 제조하여 2차 항체가 항원항체반응이 일어난 것에 결합시킨 후 효소를 첨가하여 비활성상태의 형광단백질을 활성화시켜 형광을 나타내거나 발색단백질을 이용하여 확인하는 방법, 및 항체에 발색단백질을 결합시킨 상태로 제조하여 확인하는 방법이 바람직하다. 특히 항체에 클로이달골드를 붙이고 상기 클로이달 골드가 연결된 항체가 항원항체결합물에 결합함으로써 발색반응을 나타내는 것이 더욱 바람직하다.In addition, the antigen-antibody reaction of the recombinant protein of the present invention can be carried out by a method generally performed in a laboratory. Prepared by binding the secondary antibody to the antigen antibody reaction has occurred after the addition of enzymes to activate the inactivated fluorescent protein to fluoresce or confirmed using a chromophoric protein, and the chromophore protein bound to the antibody The method of manufacturing and confirming is preferable. In particular, it is more preferable that the antibody is attached to the cloddal gold and the antibody linked to the cloddal gold exhibits a color reaction by binding to the antigen-antibody conjugate.

또한 본 발명은 상기에 설명한 유전자재조합 식품의 검출방법을 이용한 검사키트를 고안하여 실험실이나 관공서에서 쉽게 유전자변형 여부를 확인 할 수 있다. 본 발명의 EPSPS, PAT, 및 BT에 대한 검사키트를 각각 제조하여 식품에 대해 3가지 유전자의 재조합단백질을 포함하는지 여부를 확인 할 수 있다. 상기 EPSPS, PAT 및, BT의 검사키트에 포함되어지는 구성물질은 검사하고자 하는 재조합단백질의 종류에 마다 다르게 포함되어지나 사용방법은 유사하다. In addition, the present invention can devise a test kit using a method for detecting a genetically modified food described above, it is possible to easily determine whether genetic modification in a laboratory or a public office. Test kits for the EPSPS, PAT, and BT of the present invention can be prepared to determine whether the recombinant protein of three genes for food. The components included in the test kits of the EPSPS, PAT, and BT are different depending on the type of recombinant protein to be tested, but the method of use is similar.

본 발명의 유전자재조합단백질 검사키트는 통상적인 검사대와 같은 스트립(strip)키트와 엘리자(ELISA)키트가 바람직하며, 본 발명의 유전자재조합 식품의 검출방법을 이용한 여타의 검사키트를 고안하여 사용 할 수도 있다. The recombinant protein test kit of the present invention is preferably a strip kit and an ELISA kit, such as a conventional test table, and may be used to devise and use other test kits using the genetically modified food detection method of the present invention. have.

본 발명의 스트립키트는 시료의 단백질을 추출할 수 있는 단백질 추출액, 효소반응액(트립신, 키모트립신, 펩신, 섭맥실라루스 프로테이즈, St. 아우레우스 V8 프로테이즈), 본 발명에서 고안한 다른 단백질과의 상보성이 없는 펩타이드의 항체가 있는 검사용 스트립, 및 발색단이 연결된 항체를 포함한다. 상기에 대조군으로 이용하도록 유전자재조합단백질(EPSPS, BT, PAT를 함유하는 단백질군), 합성펩타이드가 결합된 단백질(BSA-, ovalbumin-, KLH-재조합단백질)를 더욱 포함할 수 있다. 검사키트는 검사하는 유전자재조합식품의 단백질을 단백질 추출액으로 추출하고, 원심분리 후 추출한 단백질을 효소반응한 다음 항체가 결합된 스트립에 젖혀서 사용하고 그 후 스트립을 발색단이 연결된 항체에 반응시켜 재조합단백질 유무를 색으로 확인한다. The strip kit of the present invention is a protein extract that can extract the protein of the sample, enzyme reaction solution (trypsin, chymotrypsin, pepsin, submaccillus protease, St. aureus V8 protease), devised in the present invention Test strips with antibodies of peptides having no complementarity with one other protein, and chromophore linked antibodies. The recombinant protein (EPSPS, BT, PAT-containing protein group), the synthetic peptide is coupled to the protein (BSA-, ovalbumin-, KLH-recombinant protein) may be further included as a control. The test kit extracts the protein from the genetically modified food to be tested with protein extract, centrifuged the enzyme and then folds the extracted protein onto the antibody-bound strip, and then reacts the strip with the chromophore-linked antibody to detect the presence of recombinant protein. Check by color.

본 발명의 엘리자(ELISA) 검사키트는 시료의 단백질을 추출할 수 있는 단백질 추출액, 효소반응액(트립신, 키모트립신, 펩신, 섭맥실라루스 프로테이즈, St. 아우레우스 V8 프로테이즈), 본 발명에서 고안한 다른 단백질과의 상보성이 없는 펩타이드의 항체가 코팅된 10-웰(well) 플레이트, 및 발색단이 연결된 항체를 포함한다. 상기에 대조군으로 이용하도록 유전자재조합단백질(EPSPS, BT, PAT를 함유하는 단백질군), 합성펩타이드가 결합된 단백질(BSA-, ovalbumin-, KLH-재조합단백질)을 더욱 포함할 수 있다.ELISA test kit of the present invention is a protein extract that can extract the protein of the sample, enzyme reaction solution (trypsin, chymotrypsin, pepsin, submaccillus protease, St. aureus V8 Protease), 10-well plates coated with antibodies of peptides having no complementarity with other proteins designed in the present invention, and chromophore linked antibodies. The recombinant protein (EPSPS, BT, PAT-containing protein group), the synthetic peptide is coupled to the protein (BSA-, ovalbumin-, KLH-recombinant protein) may be further included as a control.

상기 ELISA 검사방법은 검사하고자 하는 식품의 단백질을 추출하여 효소반응으로 분해시킨 후 항체가 프리코팅된 플레이트에 넣는다. 일정시간이 지난 다음 플레이트를 세척액으로 씻은 후 발색단이 연결된 항체를 넣어 발색여부를 확인한다. 발색이 되면 검사 식품은 유전자재조합식품이며 발색반응이 없다면 이 식품은 천연식품인 것이다. 그리고 대조군으로 유전자재조합단백질과 합성펩타이드가 결합된 단백질도 동일하게 동시에 실시한다. 유전자재조합단백질을 넣은 웰은 발색반응을 보이며 합성펩타이드를 넣은 웰은 발색반응이 없게 나타난다. In the ELISA test method, the protein of the food to be tested is decomposed by enzymatic reaction, and then put in an antibody-coated plate. After a certain period of time, the plate is washed with a washing solution, and then the chromophore-connected antibody is added to check for color development. If it develops color, the test food is a genetically modified food. If there is no color reaction, it is a natural food. As a control, the recombinant protein and the synthetic peptide are combined with the same protein. Wells containing the recombinant protein show a color reaction, while wells containing the synthetic peptide show no color reaction.

본 발명의 유전자재조합 식품의 검사키트는 상기에 기재한 필수 성분들과 더불어 그 밖의 완충용액 등이 더욱 포함되어진다.The test kit for genetically modified foods of the present invention further includes other buffer solutions, in addition to the essential components described above.

본 발명의 이해를 돕기 위하여 바람직한 실시예를 제시한다. 그러나 하기의 실시예는 본 발명을 보다 쉽게 이해하기 위하여 제공되는 것일 뿐 본 발명이 하기의 실시예에 한정되는 것은 아니다.  Preferred embodiments are presented to aid in understanding the invention. However, the following examples are provided only to more easily understand the present invention, and the present invention is not limited to the following examples.

[실시예1] EPSPS 검사법 Example 1 EPSPS Test

EPSPS의 아미노산 서열분석Amino Acid Sequencing of EPSPS

EPSPS의 아미노산서열에 대하여 트립신, 키모트립신, 펩신, St. 아우레우스(aureus) V8 프로테아제, 섭맥실라루스 프로테아제(Submaxillarus protease)의 프로테아제 절단 부위를 분석하였다. 상기 5개의 프로테아제를 각기 다른 조합으로 하여 EPSPS를 절단하였을 때 생기는 펩타이드들은 여타의 다른 단백질과 상동성분석을 실시하였다. 그 결과 트립신과 키모트립신으로 EPSPS를 분해하였을 때 하기 표 4의 5 종류의 상동성이 적은 펩타이드를 선별하였다.Trypsin, chymotrypsin, pepsin, St. The protease cleavage sites of the aureus V8 protease, Submaxillarus protease were analyzed. Peptides generated by cleaving EPSPS using the five proteases in different combinations were subjected to homology analysis with other proteins. As a result, when the EPSPS was digested with trypsin and chymotrypsin, five kinds of peptides having low homology were selected.

1One I-I-D-G-V-G-N-G-G-L-L-A-P-E-A-P-L-DI-I-D-G-V-G-N-G-G-L-L-A-P-E-A-P-L-D 22 S-A-V-L-L-A-G-L-N-T-P-G-L-T-T-V-I-E-P-I-M-TS-A-V-L-L-A-G-L-N-T-P-G-L-T-T-V-I-E-P-I-M-T 33 P-L-V-A-A-L-L-V-P-G-S-D-V-T-I-L-N-V-L-M-N-P-TP-L-V-A-A-L-L-V-P-G-S-D-V-T-I-L-N-V-L-M-N-P-T 44 T-G-L-I-L-T-L-Q-E-M-G-A-D-I-E-V-I-N-PT-G-L-I-L-T-L-Q-E-M-G-A-D-I-E-V-I-N-P 55 L-V-M-G-L-V-S-E-N-P-V-T-V-D-D-A-T-M-I-A-T-SL-V-M-G-L-V-S-E-N-P-V-T-V-D-D-A-T-M-I-A-T-S

펩타이드 합성Peptide Synthesis

상기 표 1의 5종류의 펩타이드를 Merrifield의 고체상의 펩타이드합성(SPPS; solid phase peptide synthesis)방법으로 펩트론사에서 합성하여 HPLC로 정제하여 총 5 mg을 획득하였다.Five peptides of Table 1 were synthesized by Peptron, Inc. by Merrifield's solid phase peptide synthesis (SPPS) method, and purified by HPLC to obtain a total of 5 mg.

항체제조Antibody Production

상기에서 합성한 펩타이드는 BSA(bovine serum albumin), 오발부민(ovalbumin), KLH(keyhole limpet hemocyanin)에 결합시킨 후 오드쥬번트(adjuvant)로 FCA(freund complete adjuvant)와 함께 토끼에 주사 1차 주사하고 2차, 3차로 FIA(freund incomplete adjuvant)에 혼합하여 주사하여 항체를 제작하였다. The peptide synthesized above was bound to bovine serum albumin (BSA), ovalbumin (ovalbumin), and keyhole limpet hemocyanin (KLH), and then injected into rabbits with Freund complete adjuvant (FCA) as an adjuvant. The antibody was prepared by injecting a mixture of FIA (freund incomplete adjuvant) in the second and third phases.

[실험예 1] 식품의 유전자재조합여부 검사Experimental Example 1 genetic recombination test of food

(1) 부드러운 식품(1) soft food

두부 1 g을 200 rpm에서 1분간 원심분리하여 수분을 제거한다. 수분이 제거된 두부를 효소반응액과 혼합하고 반응기에서 37 ℃에서 30분간 반응시킨 다음 원심분리하였다. 원심분리 후 상등액을 취하여 항체에 반응시킨 후 항원항체반응 유무를 발색으로 확인하였다. 1 g of tofu is centrifuged at 200 rpm for 1 minute to remove moisture. Water-free tofu was mixed with the enzyme reaction solution, reacted in a reactor at 37 ° C. for 30 minutes, and then centrifuged. After centrifugation, the supernatant was taken to react with the antibody, and the presence or absence of the antigen-antibody reaction was confirmed by color development.

(2) 딱딱한 식품(2) hard food

가공식품을 취하여 단백질추출액과 혼합하여 마쇄하였다. 마쇄액에 필요한 효소반응액을 혼합하고 반응기에 장착하여 37 ℃에서 반응시켰다. 반응액을 원심분리한 후 상등액을 취하여 항원항체반응에 의해 유전자재조합식품 여부를 확인하였다. The processed foods were taken and mixed with the protein extracts and ground. The enzyme reaction solution required for the grinding solution was mixed, mounted in a reactor, and reacted at 37 ° C. The reaction solution was centrifuged, and then the supernatant was taken to determine whether the recombinant food was produced by the antigen antibody reaction.

[실시예 2] PAT 검사Example 2 PAT inspection

PAT의 아미노산 서열분석Amino Acid Sequencing of PAT

PAT의 아미노산서열에 대하여 트립신, 키모트립신, 펩신, St. 아우레우스(aureus) V8 프로테아제, 섭맥실라루스 프로테아제(Submaxillarus protease)의 프로테아제 절단 부위를 분석하였다. 상기 5개의 프로테아제를 각기 다른 조합으로 하여 PAT를 절단하였을 때 생기는 펩타이드들은 여타의 다른 단백질과 상동성분석을 실시하였다. 그 이후의 과정은 실시예 1과 동일하다.The amino acid sequences of PAT were trypsin, chymotrypsin, pepsin, St. The protease cleavage sites of the aureus V8 protease, Submaxillarus protease were analyzed. Peptides generated by cleaving PAT using the five proteases in different combinations were subjected to homology analysis with other proteins. The subsequent procedure is the same as in Example 1.

[실시예 3] BT 검사Example 3 BT Inspection

BT의 아미노산 서열분석Amino Acid Sequencing of BT

BT의 아미노산서열에 대하여 트립신, 키모트립신, 펩신, St. 아우레우스(aureus) V8 프로테아제, 섭맥실라루스 프로테아제(Submaxillarus protease)의 프로테아제 절단 부위를 분석하였다. 상기 5개의 프로테아제를 각기 다른 조합으로 하여 BT를 절단하였을 때 생기는 펩타이드들은 여타의 다른 단백질과 상동성분석을 실시하였다. 그 이후의 과정은 실시예 1과 동일하다.Trypsin, chymotrypsin, pepsin, St. The protease cleavage sites of the aureus V8 protease, Submaxillarus protease were analyzed. Peptides generated by cleaving BT using the five proteases in different combinations were subjected to homology analysis with other proteins. The subsequent procedure is the same as in Example 1.

[실시예 4] 스트립(strip) 검사키트Example 4 Strip Inspection Kit

유전자재조합단백질(EPSPS, BT, PAT를 함유하는 단백질군), 합성펩타이드가 결합된 단백질(BSA, ovalbumin, KLH), 단백질추출액, 효소반응액(트립신, 키모트립신, 펩신, 섭맥실라루스 프로테이즈, St. 아우레우스 V8 프로테이즈), 유전자재조합단백질검사용 스트립, 항체, 발색단이 연결된 항체, 15 ml 플라스틱 원심분리관 등을 포함한다. 상기 항체는 스트립의 특정 부위에 결합되어 있어, 그 부분을 시료의 단백질 추출액과 반응시킨다.  Recombinant protein (EPSPS, BT, PAT-containing protein group), synthetic peptide-coupled protein (BSA, ovalbumin, KLH), protein extract, enzyme reaction solution (trypsin, chymotrypsin, pepsin, submacilarus protease , St. aureus V8 protease), genetically engineered protein assay strips, antibodies, chromophore linked antibodies, 15 ml plastic centrifuge tubes, and the like. The antibody is bound to a specific site of the strip and reacts that part with the protein extract of the sample.

[실험예 2] Experimental Example 2

시료에 단백질추출액을 혼합하고 원심분리로 상등액의 단백질을 수득하였다. 수득한 단백질에 효소반응을 첨가하여 반응시킨 후 스트립을 발색단이 연결된 항체에 넣어 발색반응을 확인하였다. 또한 유전자재조합단백질도 동일하게 실험하여 네그티브 대조군으로 실험하였다.The protein extract was mixed with the sample, and the supernatant was obtained by centrifugation. After the addition of the enzyme reaction to the obtained protein, the reaction was carried out by putting the strip in the chromophore-connected antibody to confirm the color reaction. Genetic recombination protein was also tested as a negative control.

[실시예 5] 엘리자(ELISA) 검사키트Example 5 ELISA Test Kit

유전자재조합단백질(EPSPS, BT, PAT를 함유하는 단백질군), 합성펩타이드가 결합된 단백질(BSA, ovalbumin, KLH), 단백질추출액, 효소반응액(트립신, 키모트립신, 펩신, 섭맥실라루스 프로테이즈, St. 아우레우스 V8 프로테이즈), ELISA용 10-웰(well) 플레이트(항체로 프리코팅되어진 플레이트), 15 ml 플라스틱 원심분리관, 1.5 ml 플라스틱 원심분리관 항원-항체 반응액, 항원-항체 반응 발색시약, 발색정지액, 세척액 등을 포함한다.Recombinant protein (EPSPS, BT, PAT-containing protein group), synthetic peptide-coupled protein (BSA, ovalbumin, KLH), protein extract, enzyme reaction solution (trypsin, chymotrypsin, pepsin, submacilarus protease , St. Aureus V8 Protease), 10-well plate (anticoated precoated plate) for ELISA, 15 ml plastic centrifuge tube, 1.5 ml plastic centrifuge tube antigen-antibody reaction solution, antigen Antibody reaction color development reagent, color stop solution, wash solution, etc.

[실험예 3] Experimental Example 3

시료에 단백질추출액을 혼합하고 원심분리로 상등액의 단백질을 수득하였다. 수득한 단백질을 효소반응을 첨가하여 반응시킨 후 10-웰 플레이트에 담아 항원항체반응을 수행하였다. 반응 후 플레이트는 세척액으로 씻은 후 발색단 용액을 첨가하고 다시 세척하여 시료를 넣은 웰의 발색여부를 확인하였다. 또한 유전자재조합단백질도 동일하게 실험하여 네그티브 대조군으로 실험하였다.The protein extract was mixed with the sample and centrifuged to obtain the supernatant protein. The obtained protein was reacted by the addition of an enzyme reaction, and then the antigen antibody reaction was carried out in a 10-well plate. After the reaction, the plate was washed with a washing solution, and then the chromophore solution was added and washed again to check whether the color of the well into which the sample was placed. Genetic recombination protein was also tested as a negative control.

상기 언급한 바와 같이 본 발명의 유전자재조합식품의 검사방법으로 재조합 유전자로 형질전환된 식물에서 재조합단백질의 발현유무를 간단하게 측정할 수 있을 뿐만 아니라 가공식품의 재조합단백질 포함여부를 쉽게 측정할 수 있다.As mentioned above, it is possible to easily measure the presence or absence of recombinant protein expression in a plant transformed with a recombinant gene by the test method of the recombinant food of the present invention, as well as to easily determine whether the recombinant protein is included in the processed food. .

<110> PARK, hee young <120> Detection method of genetic recombinant food and detection kit of that <130> dpp001057 <160> 155 <170> KOPATIN 1.5 <210> 1 <211> 31 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(31) <223> digested peptide fragment by trypsin in EPSPS protein <400> 1 Glu Gly Asp Thr Trp Ile Ile Asp Gly Val Gly Asn Gly Gly Leu Leu 1 5 10 15 Ala Pro Glu Ala Pro Leu Asp Phe Gly Asn Ala Ala Thr Gly Cys 20 25 30 <210> 2 <211> 40 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(40) <223> digested peptide fragment by trypsin in EPSPS protein <400> 2 Leu Thr Gly Gln Val Ile Asp Val Pro Gly Asp Pro Ser Ser Thr Ala 1 5 10 15 Phe Pro Leu Val Ala Ala Leu Leu Val Pro Gly Ser Asp Val Thr Ile 20 25 30 Leu Asn Val Leu Met Asn Pro Thr 35 40 <210> 3 <211> 30 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(30) <223> digested peptide fragment by trypsin in EPSPS protein <400> 3 Ala Pro Ser Met Ile Asp Glu Tyr Pro Ile Leu Ala Val Ala Ala Ala 1 5 10 15 Phe Ala Glu Gly Ala Thr Val Met Asn Gly Leu Glu Glu Leu 20 25 30 <210> 4 <211> 40 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(40) <223> digested peptide fragment by trypsin in EPSPS protein <400> 4 Ile Ala Met Ser Phe Leu Val Met Gly Leu Val Ser Glu Asn Pro Val 1 5 10 15 Thr Val Asp Asp Ala Thr Met Ile Ala Thr Ser Phe Pro Glu Phe Met 20 25 30 Asp Leu Met Ala Gly Leu Gly Ala 35 40 <210> 5 <211> 39 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(39) <223> digested peptide fragment by chemotrypsin in EPSPS protein <400> 5 Gly Gly Leu Ala Ser Gly Glu Thr Arg Ile Thr Gly Leu Leu Glu Gly 1 5 10 15 Glu Asp Val Ile Asn Thr Gly Lys Ala Met Gln Ala Met Gly Ala Arg 20 25 30 Ile Arg Lys Glu Gly Asp Thr 35 <210> 6 <211> 46 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(46) <223> digested peptide fragment by chymotrypsin in EPSPS protein <400> 6 Ile Gly Asp Ala Ser Leu Thr Lys Arg Pro Met Gly Arg Val Leu Asn 1 5 10 15 Pro Leu Arg Glu Met Gly Val Gln Val Lys Ser Glu His Gly Asp Arg 20 25 30 Leu Pro Val Thr Leu Arg Gly Pro Lys Thr Pro Thr Pro Ile 35 40 45 <210> 7 <211> 41 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(41) <223> digested peptide fragment by chymotrypsin in EPSPS protein <400> 7 Val Pro Met Ala Ser Ala Gln Val Lys Ser Ala Val Leu Leu Ala Gly 1 5 10 15 Leu Asn Thr Pro Gly Ile Thr Thr Val Ile Glu Pro Ile Met Thr Arg 20 25 30 Asp His Thr Glu Lys Met Leu Gln Gly 35 40 <210> 8 <211> 39 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(39) <223> digested peptide fragment by chymotrypsin in EPSPS protein <400> 8 Gly Ala Asn Leu Thr Val Glu Thr Asp Ala Asp Gly Val Arg Thr Ile 1 5 10 15 Arg Leu Glu Gly Arg Gly Lys Leu Thr Gly Gln Val Ile Asp Val Pro 20 25 30 Gly Asp Pro Ser Ser Thr Ala 35 <210> 9 <211> 71 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(71) <223> digested peptide fragment by chymotrypsin in EPSPS protein <400> 9 Leu Val Pro Gly Ser Asp Val Thr Ile Leu Asn Val Leu Met Asn Pro 1 5 10 15 Thr Arg Thr Gly Leu Ile Leu Thr Leu Gln Glu Met Gly Ala Asp Ile 20 25 30 Glu Val Ile Asn Pro Arg Leu Ala Gly Gly Glu Asp Val Ala Asp Leu 35 40 45 Arg Val Arg Ser Ser Thr Leu Lys Gly Val Thr Val Pro Glu Asp Arg 50 55 60 Ala Pro Ser Met Ile Asp Glu 65 70 <210> 10 <211> 72 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(72) <223> digested peptide fragment by chymotrypsin in EPSPS protein <400> 10 Ala Glu Gly Ala Thr Val Met Asn Gly Leu Glu Glu Leu Arg Val Lys 1 5 10 15 Glu Ser Asp Arg Leu Ser Ala Val Ala Asn Gly Leu Lys Leu Asn Gly 20 25 30 Val Asp Cys Asp Glu Gly Glu Thr Ser Leu Val Val Arg Gly Arg Pro 35 40 45 Asp Gly Lys Gly Leu Gly Asn Ala Ser Gly Ala Ala Val Ala Thr His 50 55 60 Leu Asp His Arg Ile Ala Met Ser 65 70 <210> 11 <211> 32 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(32) <223> digested peptide fragment by submaxillarus protease in EPSPS protein <400> 11 Lys Glu Gly Asp Thr Trp Ile Ile Asp Gly Val Gly Asn Gly Gly Leu 1 5 10 15 Leu Ala Pro Glu Ala Pro Leu Asp Phe Gly Asn Ala Ala Thr Gly Cys 20 25 30 <210> 12 <211> 31 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(31) <223> digested peptide fragment by submaxillarus protease in EPSPS protein <400> 12 Val Pro Met Ala Ser Ala Gln Val Lys Ser Ala Val Leu Leu Ala Gly 1 5 10 15 Leu Asn Thr Pro Gly Ile Thr Thr Val Ile Glu Pro Ile Met Thr 20 25 30 <210> 13 <211> 42 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(42) <223> digested peptide fragment by submaxillarus protease in EPSPS protein <400> 13 Gly Lys Leu Thr Gly Gln Val Ile Asp Val Pro Gly Asp Pro Ser Ser 1 5 10 15 Thr Ala Phe Pro Leu Val Ala Ala Leu Leu Val Pro Gly Ser Asp Val 20 25 30 Thr Ile Leu Asn Val Leu Met Asn Pro Thr 35 40 <210> 14 <211> 30 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(30) <223> digested peptide fragment by submaxillarus protease in EPSPS protein <400> 14 Ala Pro Ser Met Ile Asp Glu Tyr Pro Ile Leu Ala Val Ala Ala Ala 1 5 10 15 Phe Ala Glu Gly Ala Thr Val Met Asn Gly Leu Glu Glu Leu 20 25 30 <210> 15 <211> 24 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(24) <223> digested peptide fragment by submaxillarus protease in EPSPS protein <400> 15 Leu Ser Ala Val Ala Asn Gly Leu Lys Leu Asn Gly Val Asp Cys Asp 1 5 10 15 Glu Gly Glu Thr Ser Leu Val Val 20 <210> 16 <211> 50 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(50) <223> digested peptide fragment by submaxillarus protease in EPSPS protein <400> 16 Ile Ala Met Ser Phe Leu Val Met Gly Leu Val Ser Glu Asn Pro Val 1 5 10 15 Thr Val Asp Asp Ala Thr Met Ile Ala Thr Ser Phe Pro Glu Phe Met 20 25 30 Asp Leu Met Ala Gly Leu Gly Ala Lys Ile Glu Leu Ser Asp Thr Lys 35 40 45 Ala Ala 50 <210> 17 <211> 26 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(26) <223> digested peptide fragment by st.aureus V8 protease protease in EPSPS protein <400> 17 Met Ser His Gly Ala Ser Ser Arg Pro Ala Thr Ala Arg Lys Ser Ser 1 5 10 15 Gly Leu Ser Gly Thr Val Arg Ile Pro Gly 20 25 <210> 18 <211> 17 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(17) <223> digestional peptide by st.aureus V8 protease protease in EPSPS protein <400> 18 Val Ile Asn Thr Gly Lys Ala Met Gln Ala Met Gly Ala Arg Ile Arg 1 5 10 15 Lys <210> 19 <211> 18 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(18) <223> digested peptide fragment by st.aureus V8 protease protease in EPSPS protein <400> 19 Phe Gly Asn Ala Ala Thr Gly Cys Arg Leu Thr Met Gly Leu Val Gly 1 5 10 15 Val Tyr <210> 20 <211> 44 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(44) <223> digested peptide fragment by st.aureus V8 protease protease in EPSPS protein <400> 20 Arg Leu Pro Val Thr Leu Arg Gly Pro Lys Thr Pro Thr Pro Ile Thr 1 5 10 15 Tyr Arg Val Pro Met Ala Ser Ala Gln Val Lys Ser Ala Val Leu Leu 20 25 30 Ala Gly Leu Asn Thr Pro Gly Ile Thr Thr Val Ile 35 40 <210> 21 <211> 20 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(20) <223> digested peptide fragment by st.aureus V8 protease protease in EPSPS protein <400> 21 Val Thr Ile Leu Asn Val Leu Met Asn Pro Thr Arg Thr Gly Leu Ile 1 5 10 15 Leu Thr Leu Gln 20 <210> 22 <211> 17 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(17) <223> digested peptide fragment by trypsin and chymotrypsin in EPSPS protein <400> 22 Ile Ile Asp Gly Val Gly Asn Gly Gly Leu Leu Ala Pro Glu Ala Pro 1 5 10 15 Leu <210> 23 <211> 22 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(22) <223> digested peptide fragment by trypsin and chymotrypsin in EPSPS protein <400> 23 Ser Ala Val Leu Leu Ala Gly Leu Asn Thr Pro Gly Ile Thr Thr Val 1 5 10 15 Ile Glu Pro Ile Met Thr 20 <210> 24 <211> 23 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(23) <223> digested peptide fragment by trypsin and chymotrypsin in EPSPS protein <400> 24 Pro Leu Val Ala Ala Leu Leu Val Pro Gly Ser Asp Val Thr Ile Leu 1 5 10 15 Asn Val Leu Met Asn Pro Thr 20 <210> 25 <211> 19 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(19) <223> digested peptide fragment by trypsin and chymotrypsin in EPSPS protein <400> 25 Thr Gly Leu Ile Leu Thr Leu Gln Glu Met Gly Ala Asp Ile Glu Val 1 5 10 15 Ile Asn Pro <210> 26 <211> 16 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(16) <223> digested peptide fragment by trypsin and chymotrypsin in EPSPS protein <400> 26 Gly Leu Gly Asn Ala Ser Gly Ala Ala Val Ala Thr His Leu Asp His 1 5 10 15 <210> 27 <211> 22 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE <222> (1)..(22) <223> digested peptide fragment by trypsin and chymotrypsin in EPSPS protein <400> 27 Leu Val Met Gly Leu Val Ser Glu Asn Pro Val Thr Val Asp Asp Ala 1 5 10 15 Thr Met Ile Ala Thr Ser 20 <210> 28 <211> 25 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE <222> (1)..(22) <223> digested peptide fragment by trypsin in PATprotein <400> 28 Pro Ala Thr Ala Ala Asp Met Ala Ala Val Cys Asp Ile Val Asn His 1 5 10 15 Tyr Ile Glu Thr Ser Thr Val Asn Phe 20 25 <210> 29 <211> 14 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE <222> (1)..(14) <223> digested peptide fragment by trypsin in PATprotein <400> 29 Thr Glu Pro Gln Thr Pro Gln Glu Trp Ile Asp Asp Leu Glu 1 5 10 <210> 30 <211> 21 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE <222> (1)..(21) <223> digested peptide fragment by trypsin in PATprotein <400> 30 Tyr Pro Trp Leu Val Ala Glu Val Glu Gly Val Val Ala Gly Ile Ala 1 5 10 15 Tyr Ala Gly Pro Trp 20 <210> 31 <211> 14 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE <222> (1)..(14) <223> digested peptide fragment by chymotrypsin in PATprotein <400> 31 Val Ser His Arg His Gln Arg Leu Gly Leu Gly Ser Thr Leu 1 5 10 <210> 32 <211> 22 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE <222> (1)..(22) <223> digested peptide fragment by chymotrypsin in PATprotein <400> 32 Lys Ser Val Val Ala Val Ile Gly Leu Pro Asn Asp Pro Ser Val Arg 1 5 10 15 Leu His Glu Ala Leu Gly 20 <210> 33 <211> 18 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE <222> (1)..(18) <223> digested peptide fragment by chymotrypsin in PATprotein <400> 33 Gly Val Val Ala Gly Ile Ala Tyr Ala Gly Pro Trp Lys Ala Arg Asn 1 5 10 15 Ala Tyr <210> 34 <211> 26 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE <222> (1)..(26) <223> digested peptide fragment by st.aureus V8 protease in PAT protein <400> 34 Ser Thr Val Tyr Val Ser His Arg His Gln Arg Leu Gly Leu Gly Ser 1 5 10 15 Thr Leu Tyr Thr His Leu Leu Lys Ser Met 20 25 <210> 35 <211> 21 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE <222> (1)..(21) <223> digested peptide fragment by st.aureus V8 protease in PAT protein <400> 35 Ala Leu Gly Tyr Thr Ala Arg Gly Thr Leu Arg Ala Ala Gly Tyr Lys 1 5 10 15 His Gly Gly Trp His 20 <210> 36 <211> 25 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE <222> (1)..(25) <223> digested peptide fragment by submaxillarus protease in PAT protein <400> 36 Pro Ala Thr Ala Ala Asp Met Ala Ala Val Cys Asp Ile Val Asn His 1 5 10 15 Tyr Ile Glu Thr Ser Thr Val Asn Phe 20 25 <210> 37 <211> 23 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE <222> (1)..(23) <223> digested peptide fragment by submaxillarus protease in PAT protein <400> 37 Tyr Pro Trp Leu Val Ala Glu Val Glu Gly Val Val Ala Gly Ile Ala 1 5 10 15 Tyr Ala Gly Pro Trp Lys Ala 20 <210> 38 <211> 30 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE <222> (1)..(30) <223> digested peptide fragment by submaxillarus protease in PAT protein <400> 38 Thr Leu Tyr Thr His Leu Leu Lys Ser Met Glu Ala Gln Gly Phe Lys 1 5 10 15 Ser Val Val Ala Val Ile Gly Leu Pro Asn Asp Pro Ser Val 20 25 30 <210> 39 <211> 16 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE <222> (1)..(16) <223> digested peptide fragment by trypsin and chymotrypsin protease in PAT protein <400> 39 Pro Ala Thr Ala Ala Asp Met Ala Ala Val Cys Asp Ile Val Asn His 1 5 10 15 <210> 40 <211> 13 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE <222> (1)..(13) <223> digested peptide fragment by trypsin and chymotrypsin protease in PAT protein <400> 40 Leu Val Ala Glu Val Glu Gly Val Val Ala Gly Ile Ala 1 5 10 <210> 41 <211> 14 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE <222> (1)..(14) <223> digested peptide fragment by trypsin and chymotrypsin protease in PAT protein <400> 41 Ser Val Val Ala Val Ile Gly Leu Pro Asn Asp Pro Ser Val 1 5 10 <210> 42 <211> 24 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE <222> (1)..(24) <223> digested peptide fragment by trypsin in PAT protein <400> 42 Ala Thr Glu Ala Asp Met Pro Ala Val Cys Thr Ile Val Asn His Tyr 1 5 10 15 Ile Glu Thr Ser Thr Val Asn Phe 20 <210> 43 <211> 21 <212> PRT <213> Streptomyces hygroscopicus <400> 43 Tyr Pro Trp Leu Val Ala Glu Val Asp Gly Glu Val Ala Gly Ile Ala 1 5 10 15 Tyr Ala Gly Pro Trp 20 <210> 44 <211> 20 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE <222> (1)..(20) <223> digested peptide fragment by trypsin in PAT protein <400> 44 His Gly Asn Trp His Asp Val Gly Phe Trp Gln Ile Asp Phe Ser Leu 1 5 10 15 Pro Val Pro Pro 20 <210> 45 <211> 27 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE <222> (1)..(27) <223> digested peptide fragment by chymotrypsin in PAT protein <400> 45 Met Ser Pro Glu Arg Arg Pro Ala Asp Ile Arg Arg Ala Thr Glu Ala 1 5 10 15 Asp Met Pro Ala Val Cys Thr Ile Val Asn His 20 25 <210> 46 <211> 21 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE <222> (1)..(21) <223> digested peptide fragment by chymotrypsin in PAT protein <400> 46 Ser Val Val Ala Val Ile Gly Leu Pro Asn Asp Pro Ser Val Arg Met 1 5 10 15 His Glu Ala Leu Gly 20 <210> 47 <211> 26 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE <222> (1)..(26) <223> digested peptide fragment by st.aureus V8 in PAT protein <400> 47 Ser Thr Val Tyr Val Ser Pro Arg His Gln Arg Thr Gly Leu Gly Ser 1 5 10 15 Thr Leu Tyr Thr His Leu Leu Lys Ser Leu 20 25 <210> 48 <211> 21 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE <222> (1)..(21) <223> digested peptide fragment by st. aureus V8 protease in PAT protein <400> 48 Ala Leu Gly Tyr Ala Pro Arg Gly Met Leu Arg Ala Ala Gly Phe Lys 1 5 10 15 His Gly Asn Trp His 20 <210> 49 <211> 15 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE <222> (1)..(15) <223> digested peptide fragment by trypsin and chymotrypsin in PAT protein <400> 49 Ala Thr Glu Ala Asp Met Pro Ala Val Cys Thr Ile Val Asn His 1 5 10 15 <210> 50 <211> 14 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE <222> (1)..(14) <223> digested peptide fragment by trypsin and chymotrypsin in PAT protein <400> 50 Ser Val Val Ala Val Ile Gly Leu Pro Asn Asp Pro Ser Val 1 5 10 <210> 51 <211> 41 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(41) <223> digested peptide fragment by trypsin in MonBT protein <400> 51 Ile Gln Phe Asn Asp Met Asn Ser Ala Leu Thr Thr Ala Ile Pro Leu 1 5 10 15 Phe Ala Val Gln Asn Tyr Gln Val Pro Leu Leu Ser Val Tyr Val Gln 20 25 30 Ala Ala Asn Leu His Leu Ser Val Leu 35 40 <210> 52 <211> 25 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(25) <223> digested peptide fragment by trypsin in MonBT protein <400> 52 Gly Glu Tyr Tyr Trp Ser Gly His Gln Ile Met Ala Ser Pro Val Gly 1 5 10 15 Phe Ser Gly Ser Asn Gln Ile Gly Leu 20 25 <210> 53 <211> 26 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(26) <223> digested peptide fragment by trypsin in MonBT protein <400> 53 Thr Asp Val Thr Asp Tyr His Ile Asp Gln Val Ser Asn Leu Val Glu 1 5 10 15 Cys Leu Ser Asp Glu Phe Cys Leu Asp Glu 20 25 <210> 54 <211> 29 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(29) <223> digested peptide fragment by trypsin in MonBT protein <400> 54 Cys Ala His His Ser His His Phe Ser Leu Asp Ile Asp Val Gly Cys 1 5 10 15 Thr Asp Leu Asn Glu Asp Leu Gly Val Trp Val Ile Phe 20 25 <210> 55 <211> 25 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(25) <223> digested peptide fragment by chymotrypsin in MonBT protein <400> 55 Arg Gly Ser Ala Gln Gly Ile Glu Gly Ser Ile Arg Ser Pro His Leu 1 5 10 15 Met Asp Ile Leu Asn Ser Ile Thr Ile 20 25 <210> 56 <211> 29 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(29) <223> digested peptide fragment by chymotrypsin in MonBT protein <400> 56 Cys Leu Asp Glu Lys Lys Glu Leu Ser Glu Lys Val Lys His Ala Lys 1 5 10 15 Arg Leu Ser Asp Glu Arg Asn Leu Leu Gln Asp Pro Asn 20 25 <210> 57 <211> 18 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(18) <223> digested peptide fragment by chymotrypsin in MonBT protein <400> 57 Leu Glu Gly Arg Ala Pro Leu Val Gly Glu Ala Leu Ala Arg Gly Gln 1 5 10 15 Glu Gly <210> 58 <211> 23 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(23) <223> digested peptide fragment by submaxillarus protease in MonBT protein <400> 58 Glu Leu Thr Leu Thr Val Leu Asp Ile Val Ser Leu Phe Pro Asn Tyr 1 5 10 15 Asp Ser Pro Pro Tyr Pro Ile 20 <210> 59 <211> 64 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(64) <223> digested peptide fragment by submaxillarus protease in MonBT protein <400> 59 Gly Glu Tyr Tyr Trp Ser Gly His Gln Ile Met Ala Ser Pro Val Gly 1 5 10 15 Phe Ser Gly Ser Asn Gln Ile Gly Leu Lys Thr Asp Val Thr Asp Tyr 20 25 30 His Ile Asp Gln Val Ser Asn Leu Val Glu Cys Leu Ser Asp Glu Phe 35 40 45 Cys Leu Asp Glu Lys Lys Glu Leu Ser Glu Lys Val Lys His Ala Lys 50 55 60 <210> 60 <211> 45 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(45) <223> digested peptide fragment by submaxillarus protease in MonBT protein <400> 60 Gly Ser Thr Asp Ile Thr Ile Gln Gly Gly Asp Asp Val Phe Lys Glu 1 5 10 15 Asn Tyr Val Thr Leu Leu Gly Thr Phe Asp Glu Cys Tyr Pro Thr Tyr 20 25 30 Leu Tyr Gln Lys Ile Asp Glu Ser Lys Leu Lys Ala Tyr 35 40 45 <210> 61 <211> 65 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(65) <223> digested peptide fragment by submaxillarus protease in MonBT protein <400> 61 Tyr Asn Ala Lys His Glu Thr Val Asn Val Pro Gly Thr Gly Ser Leu 1 5 10 15 Trp Pro Leu Ser Ala Pro Ser Pro Ile Gly Lys Cys Ala His His Ser 20 25 30 His His Phe Ser Leu Asp Ile Asp Val Gly Cys Thr Asp Leu Asn Glu 35 40 45 Asp Leu Gly Val Trp Val Ile Phe Lys Ile Lys Thr Gln Asp Gly His 50 55 60 Glu 65 <210> 62 <211> 37 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(37) <223> digested peptide fragment by st.aureus protease in MonBT protein <400> 62 Met Asn Ser Ala Leu Thr Thr Ala Ile Pro Leu Phe Ala Val Gln Asn 1 5 10 15 Tyr Gln Val Pro Leu Leu Ser Val Tyr Val Gln Ala Ala Asn Leu His 20 25 30 Leu Ser Val Leu Arg 35 <210> 63 <211> 31 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(31) <223> digested peptide fragment by st.aureus protease in MonBT protein <400> 63 Thr Val Asn Val Pro Gly Thr Gly Ser Leu Trp Pro Leu Ser Ala Pro 1 5 10 15 Ser Pro Ile Gly Lys Cys Ala His His Ser His His Phe Ser Leu 20 25 30 <210> 64 <211> 13 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(13) <223> digested peptide fragment by trypsin and chymotrypsin protease in MonBT protein <400> 64 Asn Asp Met Asn Ser Ala Leu Thr Thr Ala Ile Pro Leu 1 5 10 <210> 65 <211> 13 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(13) <223> digested peptide fragment by trypsin and chymotrypsin protease in MonBT protein <400> 65 His Ile Asp Gln Val Ser Asn Leu Val Glu Cys Leu Ser 1 5 10 <210> 66 <211> 13 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(13) <223> digested peptide fragment by trypsin and chymotrypsin protease in MonBT protein <400> 66 Gly Ser Thr Asp Ile Thr Ile Gln Gly Gly Asp Asp Val 1 5 10 <210> 67 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(17) <223> digested peptide fragment by trypsin and chymotrypsin protease in MonBT protein <400> 67 Ser Leu Asp Ile Asp Val Gly Cys Thr Asp Leu Asn Glu Asp Leu Gly 1 5 10 15 Val <210> 68 <211> 58 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(58) <223> digested peptide fragment by trypsin in cry1 protein <400> 68 Ile Glu Thr Gly Tyr Thr Pro Ile Asp Ile Ser Leu Ser Leu Thr Gln 1 5 10 15 Phe Leu Leu Ser Glu Phe Val Pro Gly Ala Gly Phe Val Leu Gly Leu 20 25 30 Val Asp Ile Ile Trp Gly Ile Phe Gly Pro Ser Gln Trp Asp Ala Phe 35 40 45 Leu Val Gln Ile Glu Gln Leu Ile Asn Gln 50 55 <210> 69 <211> 47 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(47) <223> digested peptide fragment by trypsin in cry1 protein <400> 69 Gly Phe Asn Tyr Trp Ser Gly His Gln Ile Thr Thr Ser Pro Val Gly 1 5 10 15 Phe Ser Gly Pro Glu Phe Ala Phe Pro Leu Phe Gly Asn Ala Gly Asn 20 25 30 Ala Ala Pro Pro Val Leu Val Ser Leu Thr Gly Leu Gly Ile Phe 35 40 45 <210> 70 <211> 34 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(34) <223> digested peptide fragment by trypsin in cry1 protein <400> 70 Ile Ile Leu Gly Ser Gly Pro Asn Asn Gln Glu Leu Phe Val Leu Asp 1 5 10 15 Gly Thr Glu Phe Ser Phe Ala Ser Leu Thr Thr Asn Leu Pro Ser Thr 20 25 30 Ile Tyr <210> 71 <211> 33 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(33) <223> digested peptide fragment by trypsin in cry1 protein <400> 71 Thr Val Gly Phe Thr Thr Pro Phe Asn Phe Ser Asn Gly Ser Ser Val 1 5 10 15 Phe Thr Leu Ser Ala His Val Phe Asn Ser Gly Asn Glu Val Tyr Ile 20 25 30 Asp <210> 72 <211> 26 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(26) <223> digested peptide fragment by trypsin in cry1 protein <400> 72 Thr Asp Gly Thr Asp Tyr His Ile Asp Gln Val Ser Asn Leu Val Glu 1 5 10 15 Cys Leu Ser Asp Glu Phe Cys Leu Asp Glu 20 25 <210> 73 <211> 29 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(29) <223> digested peptide fragment by trypsin in cry1 protein <400> 73 Cys Ala His His Ser His His Phe Ser Leu Asp Ile Asp Val Gly Cys 1 5 10 15 Thr Asp Leu Asn Glu Asp Leu Gly Val Trp Val Ile Phe 20 25 <210> 74 <211> 28 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(28) <223> digested peptide fragment by trypsin in cry1 protein <400> 74 Glu Ser Val Asp Ala Leu Phe Val Asn Ser Gln Tyr Asp Gln Leu Gln 1 5 10 15 Ala Asp Thr Asn Ile Ala Met Ile His Ala Ala Asp 20 25 <210> 75 <211> 23 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(23) <223> digested peptide fragment by trypsin in cry1 protein <400> 75 Glu Ala Tyr Leu Pro Glu Leu Ser Val Ile Pro Gly Val Asn Ala Ala 1 5 10 15 Ile Phe Glu Glu Leu Glu Gly 20 <210> 76 <211> 33 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(33) <223> digested peptide fragment by trypsin in cry1 protein <400> 76 Phe Ser Asn Cys Val Glu Glu Glu Ile Tyr Pro Asn Asn Thr Val Thr 1 5 10 15 Cys Asn Asp Tyr Thr Val Asn Gln Glu Glu Tyr Gly Gly Ala Tyr Thr 20 25 30 Ser <210> 77 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(19) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 77 Gly Asn Ala Gly Asn Ala Ala Pro Pro Val Leu Val Ser Leu Thr Gly 1 5 10 15 Leu Gly Ile <210> 78 <211> 24 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(24) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 78 Arg Gln Arg Gly Thr Val Asp Ser Leu Asp Val Ile Pro Pro Gln Asp 1 5 10 15 Asn Ser Val Pro Pro Arg Ala Gly 20 <210> 79 <211> 21 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(21) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 79 Gln Ile Pro Leu Thr Lys Ser Thr Asn Leu Gly Ser Gly Thr Ser Val 1 5 10 15 Val Lys Gly Pro Gly 20 <210> 80 <211> 28 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(28) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 80 Thr Gly Gly Asp Ile Leu Arg Arg Thr Ser Pro Gly Leu Ile Ser Thr 1 5 10 15 Leu Arg Val Asn Ile Thr Ala Pro Leu Ser Gln Arg 20 25 <210> 81 <211> 15 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(15) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 81 His Ile Asp Gln Val Ser Asn Leu Val Glu Cys Leu Ser Asp Glu 1 5 10 15 <210> 82 <211> 29 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(29) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 82 Cys Leu Asp Glu Lys Gln Glu Leu Ser Glu Lys Val Lys His Ala Lys 1 5 10 15 Arg Leu Ser Asp Glu Arg Asn Leu Leu Gln Asp Pro Asn 20 25 <210> 83 <211> 22 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(22) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 83 Pro Val Ser Ala Pro Lys Pro Ile Gly Lys Cys Gly Glu Pro Asn Arg 1 5 10 15 Cys Ala Pro His Leu Glu 20 <210> 84 <211> 20 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(20) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 84 Asn Pro Asp Leu Asp Cys Ser Cys Arg Asp Gly Glu Lys Cys Ala His 1 5 10 15 His Ser His His 20 <210> 85 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(17) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 85 Ser Leu Asp Ile Asp Val Gly Cys Thr Asp Leu Asn Glu Asp Leu Gly 1 5 10 15 Val <210> 86 <211> 16 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(16) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 86 Asp Gln Leu Gln Ala Asp Thr Asn Ile Ala Met Ile His Ala Ala Asp 1 5 10 15 <210> 87 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(17) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 87 Gly Glu Gly Cys Val Thr Ile His Glu Ile Glu Asn Asn Thr Asp Glu 1 5 10 15 Leu <210> 88 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(19) <223> digested peptide fragment by trypsin and chymotrypsin in cry1 protein <400> 88 Gly Asn Ala Gly Asn Ala Ala Pro Pro Val Leu Val Ser Leu Thr Gly 1 5 10 15 Leu Gly Ile <210> 89 <211> 18 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(18) <223> digested peptide fragment by trypsin and chymotrypsin in cry1 protein <400> 89 Gly Thr Val Asp Ser Leu Asp Val Ile Pro Pro Gln Asp Asn Ser Val 1 5 10 15 Pro Pro <210> 90 <211> 15 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(15) <223> digested peptide fragment by trypsin and chymotrypsin in cry1 protein <400> 90 His Ile Asp Gln Val Ser Asn Leu Val Glu Cys Leu Ser Asp Glu 1 5 10 15 <210> 91 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(17) <223> digested peptide fragment by trypsin and chymotrypsin and in cry1 protein <400> 91 Ser Leu Asp Ile Asp Val Gly Cys Thr Asp Leu Asn Glu Asp Leu Gly 1 5 10 15 Val <210> 92 <211> 16 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(16) <223> digested peptide fragment by trypsin and chymotrypsin and in cry1 protein <400> 92 Asp Gln Leu Gln Ala Asp Thr Asn Ile Ala Met Ile His Ala Ala Asp 1 5 10 15 <210> 93 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(17) <223> digested peptide fragment by trypsin and chymotrypsin in cry1 protein <400> 93 Gly Glu Gly Cys Val Thr Ile His Glu Ile Glu Asn Asn Thr Asp Glu 1 5 10 15 Leu <210> 94 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(19) <223> digested peptide fragment by trypsin in cryBI protein <400> 94 Thr Asp His Ser Leu Tyr Val Ala Pro Val Val Gly Thr Val Ser Ser 1 5 10 15 Phe Leu Leu <210> 95 <211> 33 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(33) <223> digested peptide fragment by trypsin in cryBI protein <400> 95 Glu Phe Asn Gln Gln Val Asp Asn Phe Leu Asn Pro Thr Gln Asn Pro 1 5 10 15 Val Pro Leu Ser Ile Thr Ser Ser Val Asn Thr Met Gln Gln Leu Phe 20 25 30 Leu <210> 96 <211> 28 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(28) <223> digested peptide fragment by trypsin in cryBI protein <400> 96 Leu Pro Gln Phe Gln Ile Gln Gly Tyr Gln Leu Leu Leu Leu Pro Leu 1 5 10 15 Phe Ala Gln Ala Ala Asn Met His Leu Ser Phe Ile 20 25 <210> 97 <211> 51 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(51) <223> digested peptide fragment by trypsin in cryBI protein <400> 97 Tyr Gln Ser Leu Met Val Ser Ser Gly Ala Asn Leu Tyr Ala Ser Gly 1 5 10 15 Ser Gly Pro Gln Gln Thr Gln Ser Phe Thr Ala Gln Asn Trp Pro Phe 20 25 30 Leu Tyr Ser Leu Phe Gln Val Asn Ser Asn Tyr Ile Leu Ser Gly Ile 35 40 45 Ser Gly Thr 50 <210> 98 <211> 35 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(35) <223> digested peptide fragment by trypsin in cryBI protein <400> 98 Val Asn Tyr Ser Gly Gly Val Ser Ser Gly Leu Ile Gly Ala Thr Asn 1 5 10 15 Leu Asn His Asn Phe Asn Cys Ser Thr Val Leu Pro Pro Leu Ser Thr 20 25 30 Pro Phe Val 35 <210> 99 <211> 37 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(37) <223> digested peptide fragment by trypsin in cryBI protein <400> 99 Asn Asn Ile Tyr Ala Ala Asn Glu Asn Gly Thr Met Ile His Leu Ala 1 5 10 15 Pro Glu Asp Tyr Thr Gly Phe Thr Ile Ser Pro Ile His Ala Thr Gln 20 25 30 Val Asn Asn Gln Thr 35 <210> 100 <211> 27 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(27) <223> digested peptide fragment by trypsin in cryBI protein <400> 100 Val Thr Ile Asn Gly Arg Val Tyr Thr Val Ser Asn Val Asn Thr Thr 1 5 10 15 Thr Asn Asn Asp Gly Val Asn Asp Asn Gly Ala 20 25 <210> 101 <211> 47 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(47) <223> digested peptide fragment by trypsin in cryBI protein <400> 101 Phe Ser Asp Ile Asn Ile Gly Asn Ile Val Ala Ser Asp Asn Thr Asn 1 5 10 15 Val Thr Leu Asp Ile Asn Val Thr Leu Asn Ser Gly Thr Pro Phe Asp 20 25 30 Leu Met Asn Ile Met Phe Val Pro Thr Asn Leu Pro Pro Leu Tyr 35 40 45 <210> 102 <211> 22 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(22) <223> digested peptide fragment by trypsin and chymotrypsin in cryBI protein <400> 102 Leu Asn Pro Thr Gln Asn Pro Val Pro Leu Ser Ile Thr Ser Ser Val 1 5 10 15 Asn Thr Met Gln Gln Leu 20 <210> 103 <211> 18 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(18) <223> digested peptide fragment by trypsin and chymotrypsin in cryBI protein <400> 103 Pro Asn Ile Gly Gly Leu Pro Gly Ser Thr Thr Thr His Ser Leu Asn 1 5 10 15 Ser Ala <210> 104 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(19) <223> digested peptide fragment by trypsin and chymotrypsin in cryBI protein <400> 104 Thr Val Ser Asn Val Asn Thr Thr Thr Asn Asn Asp Gly Val Asn Asp 1 5 10 15 Asn Gly Ala <210> 105 <211> 29 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(29) <223> digested peptide fragment by trypsin and chymotrypsin in cryBI protein <400> 105 Ser Asp Ile Asn Ile Gly Asn Ile Val Ala Ser Asp Asn Thr Asn Val 1 5 10 15 Thr Leu Asp Ile Asn Val Thr Leu Asn Ser Gly Thr Pro 20 25 <210> 106 <211> 58 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(58) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 106 Ile Glu Thr Gly Tyr Thr Pro Ile Asp Ile Ser Leu Ser Leu Thr Gln 1 5 10 15 Phe Leu Leu Ser Glu Phe Val Pro Gly Ala Gly Phe Val Leu Gly Leu 20 25 30 Val Asp Ile Ile Trp Gly Ile Phe Gly Pro Ser Gln Trp Asp Ala Phe 35 40 45 Leu Val Gln Ile Glu Gln Leu Ile Asn Gln 50 55 <210> 107 <211> 41 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(41) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 107 Ile Gln Phe Asn Asp Met Asn Ser Ala Leu Thr Thr Ala Ile Pro Leu 1 5 10 15 Phe Ala Val Gln Asn Tyr Gln Val Pro Leu Leu Ser Val Tyr Val Gln 20 25 30 Ala Ala Asn Leu His Leu Ser Val Leu 35 40 <210> 108 <211> 32 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(32) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 108 Pro Phe Asn Ile Gly Ile Asn Asn Gln Gln Leu Ser Val Leu Asp Gly 1 5 10 15 Thr Glu Phe Ala Tyr Gly Thr Ser Ser Asn Leu Pro Ser Ala Val Tyr 20 25 30 <210> 109 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(19) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 109 Ser Gly Thr Val Asp Ser Leu Asp Glu Ile Pro Pro Gln Asn Asn Asn 1 5 10 15 Val Pro Pro <210> 110 <211> 33 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(33) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 110 Thr Val Gly Phe Thr Thr Pro Phe Asn Phe Ser Asn Gly Ser Ser Val 1 5 10 15 Phe Thr Leu Ser Ala His Val Phe Asn Ser Gly Asn Glu Val Tyr Ile 20 25 30 Asp <210> 111 <211> 26 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(26) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 111 Thr Asp Val Thr Asp Tyr His Ile Asp Gln Val Ser Asn Leu Val Glu 1 5 10 15 Cys Leu Ser Asp Glu Phe Cys Leu Asp Glu 20 25 <210> 112 <211> 25 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(25) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 112 Ser His His Phe Ser Leu Asp Ile Asp Val Gly Cys Thr Asp Leu Asn 1 5 10 15 Glu Asp Leu Gly Val Trp Val Ile Phe 20 25 <210> 113 <211> 23 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(23) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 113 Glu Ala Tyr Leu Pro Glu Leu Ser Val Ile Pro Gly Val Asn Ala Ala 1 5 10 15 Ile Phe Glu Glu Leu Glu Gly 20 <210> 114 <211> 32 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(32) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 114 Ser Asn Cys Val Glu Glu Glu Val Tyr Pro Asn Asn Thr Val Thr Cys 1 5 10 15 Asn Asp Tyr Thr Ala Thr Gln Glu Glu Tyr Glu Gly Thr Tyr Thr Ser 20 25 30 <210> 115 <211> 25 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(25) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 115 Arg Gly Ser Ala Gln Gly Ile Glu Gly Ser Ile Arg Ser Pro His Leu 1 5 10 15 Met Asp Ile Leu Asn Ser Ile Thr Ile 20 25 <210> 116 <211> 20 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(20) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 116 Gly Thr Met Gly Asn Ala Ala Pro Gln Gln Arg Ile Val Ala Gln Leu 1 5 10 15 Gly Gln Gly Val 20 <210> 117 <211> 24 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(24) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 117 Arg Lys Ser Gly Thr Val Asp Ser Leu Asp Glu Ile Pro Pro Gln Asn 1 5 10 15 Asn Asn Val Pro Pro Arg Gln Gly 20 <210> 118 <211> 31 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(31) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 118 Asn Asn Ile Ile Pro Ser Ser Gln Ile Thr Gln Ile Pro Leu Thr Lys 1 5 10 15 Ser Thr Asn Leu Gly Ser Gly Thr Ser Val Val Lys Gly Pro Gly 20 25 30 <210> 119 <211> 27 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(27) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 119 Gly Gly Asp Ile Leu Arg Arg Thr Ser Pro Gly Gln Ile Ser Thr Leu 1 5 10 15 Arg Val Asn Ile Thr Ala Pro Leu Ser Gln Arg 20 25 <210> 120 <211> 29 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(29) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 120 Cys Leu Asp Glu Lys Lys Glu Leu Ser Glu Lys Val Lys His Ala Lys 1 5 10 15 Arg Leu Ser Asp Glu Arg Asn Leu Leu Gln Asp Pro Asn 20 25 <210> 121 <211> 23 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(23) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 121 Asp Arg Leu Gln Ala Asp Thr Asn Ile Ala Met Ile His Ala Ala Asp 1 5 10 15 Lys Arg Val His Ser Ile Arg 20 <210> 122 <211> 22 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(22) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 122 Asn Val Lys Gly His Val Asp Val Glu Glu Gln Asn Asn His Arg Ser 1 5 10 15 Val Leu Val Val Pro Glu 20 <210> 123 <211> 16 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(16) <223> digested peptide fragment by trypsin and chymotrypsin in cryHD-1 protein <400> 123 Asn Ile Gly Ile Asn Asn Gln Gln Leu Ser Val Leu Asp Gly Thr Glu 1 5 10 15 <210> 124 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(19) <223> digested peptide fragment by trypsin and chymotrypsin in cryHD-1 protein <400> 124 Ser Gly Thr Val Asp Ser Leu Asp Glu Ile Pro Pro Gln Asn Asn Asn 1 5 10 15 Val Pro Pro <210> 125 <211> 14 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(14) <223> digested peptide fragment by trypsin and chymotrypsin in cryHD-1 protein <400> 125 Ser Ala Thr Met Ser Ser Gly Ser Asn Leu Gln Ser Gly Ser 1 5 10 <210> 126 <211> 15 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(15) <223> digested peptide fragment by trypsin and chymotrypsin in cryHD-1 protein <400> 126 His Ile Asp Gln Val Ser Asn Leu Val Glu Cys Leu Ser Asp Glu 1 5 10 15 <210> 127 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(17) <223> digested peptide fragment by trypsin and chymotrypsin in cryHD-1 protein <400> 127 Ser Leu Asp Ile Asp Val Gly Cys Thr Asp Leu Asn Glu Asp Leu Gly 1 5 10 15 Val <210> 128 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(17) <223> digested peptide fragment by trypsin and chymotrypsin in cryHD-1 protein <400> 128 Gly Glu Gly Cys Val Thr Ile His Glu Ile Glu Asn Asn Thr Asp Glu 1 5 10 15 Leu <210> 129 <211> 38 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(38) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 129 Gly Ile Ser Val Val Gly Asp Leu Leu Gly Val Val Gly Phe Pro Phe 1 5 10 15 Gly Gly Ala Leu Val Ser Phe Tyr Thr Asn Phe Leu Asn Thr Ile Trp 20 25 30 Pro Ser Glu Asp Pro Trp 35 <210> 130 <211> 21 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(21) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 130 Ala Leu Ala Glu Leu Gln Gly Leu Gln Asn Asn Val Glu Asp Tyr Val 1 5 10 15 Ser Ala Leu Ser Ser 20 <210> 131 <211> 29 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(29) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 131 Asn Ser Met Pro Ser Phe Ala Ile Ser Gly Tyr Glu Val Leu Phe Leu 1 5 10 15 Thr Thr Tyr Ala Gln Ala Ala Asn Thr His Leu Phe Leu 20 25 <210> 132 <211> 21 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(21) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 132 Phe Gln Pro Gly Tyr Tyr Gly Asn Asp Ser Phe Asn Tyr Trp Ser Gly 1 5 10 15 Asn Tyr Val Ser Thr 20 <210> 133 <211> 20 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(20) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 133 Val Glu Phe Ser Gln Tyr Asn Asp Gln Thr Asp Glu Ala Ser Thr Gln 1 5 10 15 Thr Tyr Asp Ser 20 <210> 134 <211> 23 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(23) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 134 Asn Val Gly Ala Val Ser Trp Asp Ser Ile Asp Gln Leu Pro Pro Glu 1 5 10 15 Thr Thr Asp Glu Pro Leu Glu 20 <210> 135 <211> 28 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(28) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 135 Phe Thr Gly Gly Asp Ile Ile Gln Cys Thr Glu Asn Gly Ser Ala Ala 1 5 10 15 Thr Ile Tyr Val Thr Pro Asp Val Ser Tyr Ser Gln 20 25 <210> 136 <211> 26 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(26) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 136 Ile His Tyr Ala Ser Thr Ser Gln Ile Thr Phe Thr Leu Ser Leu Asp 1 5 10 15 Gly Ala Pro Phe Asn Gln Tyr Tyr Phe Asp 20 25 <210> 137 <211> 36 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(36) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 137 Gly Asp Thr Leu Thr Tyr Asn Ser Phe Asn Leu Ala Ser Phe Ser Thr 1 5 10 15 Pro Phe Glu Leu Ser Gly Asn Asn Leu Gln Ile Gly Val Thr Gly Leu 20 25 30 Ser Ala Gly Asp 35 <210> 138 <211> 18 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(18) <223> digested peptide fragment by chymotrypsin in cryIIIA protein <400> 138 Ala Lys Asn Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln Asn Asn Val 1 5 10 15 Glu Asp <210> 139 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(19) <223> digested peptide fragment by chymotrypsin in cryIIIA protein <400> 139 Gln Lys Asn Pro Val Ser Ser Arg Asn Pro His Ser Gln Gly Arg Ile 1 5 10 15 Arg Glu Leu <210> 140 <211> 18 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(18) <223> digested peptide fragment by chymotrypsin in cryIIIA protein <400> 140 Asp Ser Ile Asp Gln Leu Pro Pro Glu Thr Thr Asp Glu Pro Leu Glu 1 5 10 15 Lys Gly <210> 141 <211> 20 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(20) <223> digested peptide fragment by chymotrypsin in cryIIIA protein <400> 141 Glu Leu Ser Gly Asn Asn Leu Gln Ile Gly Val Thr Gly Leu Ser Ala 1 5 10 15 Gly Asp Lys Val 20 <210> 142 <211> 28 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(28) <223> digested peptide fragment by submaxillarus protease in cryIIIA protein <400> 142 Leu Leu Gly Val Val Gly Phe Pro Phe Gly Gly Ala Leu Val Ser Phe 1 5 10 15 Tyr Thr Asn Phe Leu Asn Thr Ile Trp Pro Ser Glu 20 25 <210> 143 <211> 67 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(67) <223> digested peptide fragment by submaxillarus protease in cryIIIA protein <400> 143 Tyr Val Ser Ala Leu Ser Ser Trp Gln Lys Asn Pro Val Ser Ser Arg 1 5 10 15 Asn Pro His Ser Gln Gly Arg Ile Arg Glu Leu Phe Ser Gln Ala Glu 20 25 30 Ser His Phe Arg Asn Ser Met Pro Ser Phe Ala Ile Ser Gly Tyr Glu 35 40 45 Val Leu Phe Leu Thr Thr Tyr Ala Gln Ala Ala Asn Thr His Leu Phe 50 55 60 Leu Leu Lys 65 <210> 144 <211> 54 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(54) <223> digested peptide fragment by submaxillarus protease in cryIIIA protein <400> 144 Ile Ile Thr Ser Pro Phe Tyr Gly Asn Lys Ser Ser Glu Pro Val Gln 1 5 10 15 Asn Leu Glu Phe Asn Gly Glu Lys Val Tyr Arg Ala Val Ala Asn Thr 20 25 30 Asn Leu Ala Val Trp Pro Ser Ala Val Tyr Ser Gly Val Thr Lys Val 35 40 45 Glu Phe Ser Gln Tyr Asn 50 <210> 145 <211> 35 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(35) <223> digested peptide fragment by submaxillarus protease in cryIIIA protein <400> 145 Glu Pro Leu Glu Lys Gly Tyr Ser His Gln Leu Asn Tyr Val Met Cys 1 5 10 15 Phe Leu Met Gln Gly Ser Arg Gly Thr Ile Pro Val Leu Thr Trp Thr 20 25 30 His Lys Ser 35 <210> 146 <211> 30 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(30) <223> digested peptide fragment by submaxillarus protease in cryIIIA protein <400> 146 Ser Lys Lys Ile Thr Gln Leu Pro Leu Val Lys Ala Tyr Lys Leu Gln 1 5 10 15 Ser Gly Ala Ser Val Val Ala Gly Pro Arg Phe Thr Gly Gly 20 25 30 <210> 147 <211> 25 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(25) <223> digested peptide fragment by submaxillarus protease in cryIIIA protein <400> 147 Val Ser Tyr Ser Gln Lys Tyr Arg Ala Arg Ile His Tyr Ala Ser Thr 1 5 10 15 Ser Gln Ile Thr Phe Thr Leu Ser Leu 20 25 <210> 148 <211> 33 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(33) <223> digested peptide fragment by submaxillarus protease in cryIIIA protein <400> 148 Thr Leu Thr Tyr Asn Ser Phe Asn Leu Ala Ser Phe Ser Thr Pro Phe 1 5 10 15 Glu Leu Ser Gly Asn Asn Leu Gln Ile Gly Val Thr Gly Leu Ser Ala 20 25 30 Gly <210> 149 <211> 27 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(27) <223> digested peptide fragment by st.aureus V8 protease in cryIIIA protein <400> 149 Leu Leu Gly Val Val Gly Phe Pro Phe Gly Gly Ala Leu Val Ser Phe 1 5 10 15 Tyr Thr Asn Phe Leu Asn Thr Ile Trp Pro Ser 20 25 <210> 150 <211> 25 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(25) <223> digested peptide fragment by st.aureus V8 protease in cryIIIA protein <400> 150 Tyr Val Ser Ala Leu Ser Ser Trp Gln Lys Asn Pro Val Ser Ser Arg 1 5 10 15 Asn Pro His Ser Gln Gly Arg Ile Arg 20 25 <210> 151 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(19) <223> digested peptide fragment by st.aureus V8 protease in cryIIIA protein <400> 151 Val Leu Phe Leu Thr Thr Tyr Ala Gln Ala Ala Asn Thr His Leu Phe 1 5 10 15 Leu Leu Lys <210> 152 <211> 31 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(31) <223> digested peptide fragment by st.aureus V8 protease in cryIIIA protein <400> 152 Lys Gly Tyr Ser His Gln Leu Asn Tyr Val Met Cys Phe Leu Met Gln 1 5 10 15 Gly Ser Arg Gly Thr Ile Pro Val Leu Thr Trp Thr His Lys Ser 20 25 30 <210> 153 <211> 30 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(30) <223> digested peptide fragment by st.aureus V8 protease in cryIIIA protein <400> 153 Ser Lys Lys Ile Thr Gln Leu Pro Leu Val Lys Ala Tyr Lys Leu Gln 1 5 10 15 Ser Gly Ala Ser Val Val Ala Gly Pro Arg Phe Thr Gly Gly 20 25 30 <210> 154 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(17) <223> digested peptide fragment by trypsin and chymotrypsin protease in cryIIIA protein <400> 154 Thr Gly Gly Asp Ile Ile Gln Cys Thr Glu Asn Gly Ser Ala Ala Thr 1 5 10 15 Ile <210> 155 <211> 18 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE <222> (1)..(18) <223> digested peptide fragment by trypsin and chymotrypsin protease in cryIIIA protein <400> 155 Glu Leu Ser Gly Asn Asn Leu Gln Ile Gly Val Thr Gly Leu Ser Ala 1 5 10 15 Gly Asp<110> PARK, hee young <120> Detection method of genetic recombinant food and detection kit of that <130> dpp001057 <160> 155 <170> KOPATIN 1.5 <210> 1 <211> 31 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (31) <223> digested peptide fragment by trypsin in EPSPS protein <400> 1 Glu Gly Asp Thr Trp Ile Ile Asp Gly Val Gly Asn Gly Gly Leu Leu 1 5 10 15 Ala Pro Glu Ala Pro Leu Asp Phe Gly Asn Ala Ala Thr Gly Cys 20 25 30 <210> 2 <211> 40 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (40) <223> digested peptide fragment by trypsin in EPSPS protein <400> 2 Leu Thr Gly Gln Val Ile Asp Val Pro Gly Asp Pro Ser Ser Thr Ala 1 5 10 15 Phe Pro Leu Val Ala Ala Leu Leu Val Pro Gly Ser Asp Val Thr Ile 20 25 30 Leu Asn Val Leu Met Asn Pro Thr 35 40 <210> 3 <211> 30 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (30) <223> digested peptide fragment by trypsin in EPSPS protein <400> 3 Ala Pro Ser Met Ile Asp Glu Tyr Pro Ile Leu Ala Val Ala Ala Ala 1 5 10 15 Phe Ala Glu Gly Ala Thr Val Met Asn Gly Leu Glu Glu Leu 20 25 30 <210> 4 <211> 40 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (40) <223> digested peptide fragment by trypsin in EPSPS protein <400> 4 Ile Ala Met Ser Phe Leu Val Met Gly Leu Val Ser Glu Asn Pro Val 1 5 10 15 Thr Val Asp Asp Ala Thr Met Ile Ala Thr Ser Phe Pro Glu Phe Met 20 25 30 Asp Leu Met Ala Gly Leu Gly Ala 35 40 <210> 5 <211> 39 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (39) <223> digested peptide fragment by chemotrypsin in EPSPS protein <400> 5 Gly Gly Leu Ala Ser Gly Glu Thr Arg Ile Thr Gly Leu Leu Glu Gly 1 5 10 15 Glu Asp Val Ile Asn Thr Gly Lys Ala Met Gln Ala Met Gly Ala Arg 20 25 30 Ile Arg Lys Glu Gly Asp Thr 35 <210> 6 <211> 46 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (46) <223> digested peptide fragment by chymotrypsin in EPSPS protein <400> 6 Ile Gly Asp Ala Ser Leu Thr Lys Arg Pro Met Gly Arg Val Leu Asn 1 5 10 15 Pro Leu Arg Glu Met Gly Val Gln Val Lys Ser Glu His Gly Asp Arg 20 25 30 Leu Pro Val Thr Leu Arg Gly Pro Lys Thr Pro Thr Pro Ile 35 40 45 <210> 7 <211> 41 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (41) <223> digested peptide fragment by chymotrypsin in EPSPS protein <400> 7 Val Pro Met Ala Ser Ala Gln Val Lys Ser Ala Val Leu Leu Ala Gly 1 5 10 15 Leu Asn Thr Pro Gly Ile Thr Thr Val Ile Glu Pro Ile Met Thr Arg 20 25 30 Asp His Thr Glu Lys Met Leu Gln Gly 35 40 <210> 8 <211> 39 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (39) <223> digested peptide fragment by chymotrypsin in EPSPS protein <400> 8 Gly Ala Asn Leu Thr Val Glu Thr Asp Ala Asp Gly Val Arg Thr Ile 1 5 10 15 Arg Leu Glu Gly Arg Gly Lys Leu Thr Gly Gln Val Ile Asp Val Pro 20 25 30 Gly Asp Pro Ser Ser Thr Ala 35 <210> 9 <211> 71 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (71) <223> digested peptide fragment by chymotrypsin in EPSPS protein <400> 9 Leu Val Pro Gly Ser Asp Val Thr Ile Leu Asn Val Leu Met Asn Pro 1 5 10 15 Thr Arg Thr Gly Leu Ile Leu Thr Leu Gln Glu Met Gly Ala Asp Ile 20 25 30 Glu Val Ile Asn Pro Arg Leu Ala Gly Gly Glu Asp Val Ala Asp Leu 35 40 45 Arg Val Arg Ser Ser Thr Leu Lys Gly Val Thr Val Pro Glu Asp Arg 50 55 60 Ala Pro Ser Met Ile Asp Glu 65 70 <210> 10 <211> 72 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (72) <223> digested peptide fragment by chymotrypsin in EPSPS protein <400> 10 Ala Glu Gly Ala Thr Val Met Asn Gly Leu Glu Glu Leu Arg Val Lys 1 5 10 15 Glu Ser Asp Arg Leu Ser Ala Val Ala Asn Gly Leu Lys Leu Asn Gly 20 25 30 Val Asp Cys Asp Glu Gly Glu Thr Ser Leu Val Val Arg Gly Arg Pro 35 40 45 Asp Gly Lys Gly Leu Gly Asn Ala Ser Gly Ala Ala Val Ala Thr His 50 55 60 Leu Asp His Arg Ile Ala Met Ser 65 70 <210> 11 <211> 32 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (32) <223> digested peptide fragment by submaxillarus protease in EPSPS protein <400> 11 Lys Glu Gly Asp Thr Trp Ile Ile Asp Gly Val Gly Asn Gly Gly Leu 1 5 10 15 Leu Ala Pro Glu Ala Pro Leu Asp Phe Gly Asn Ala Ala Thr Gly Cys 20 25 30 <210> 12 <211> 31 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (31) <223> digested peptide fragment by submaxillarus protease in EPSPS protein <400> 12 Val Pro Met Ala Ser Ala Gln Val Lys Ser Ala Val Leu Leu Ala Gly 1 5 10 15 Leu Asn Thr Pro Gly Ile Thr Thr Val Ile Glu Pro Ile Met Thr 20 25 30 <210> 13 <211> 42 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (42) <223> digested peptide fragment by submaxillarus protease in EPSPS protein <400> 13 Gly Lys Leu Thr Gly Gln Val Ile Asp Val Pro Gly Asp Pro Ser Ser 1 5 10 15 Thr Ala Phe Pro Leu Val Ala Ala Leu Leu Val Pro Gly Ser Asp Val 20 25 30 Thr Ile Leu Asn Val Leu Met Asn Pro Thr 35 40 <210> 14 <211> 30 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (30) <223> digested peptide fragment by submaxillarus protease in EPSPS protein <400> 14 Ala Pro Ser Met Ile Asp Glu Tyr Pro Ile Leu Ala Val Ala Ala Ala 1 5 10 15 Phe Ala Glu Gly Ala Thr Val Met Asn Gly Leu Glu Glu Leu 20 25 30 <210> 15 <211> 24 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (24) <223> digested peptide fragment by submaxillarus protease in EPSPS protein <400> 15 Leu Ser Ala Val Ala Asn Gly Leu Lys Leu Asn Gly Val Asp Cys Asp 1 5 10 15 Glu Gly Glu Thr Ser Leu Val Val 20 <210> 16 <211> 50 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (50) <223> digested peptide fragment by submaxillarus protease in EPSPS protein <400> 16 Ile Ala Met Ser Phe Leu Val Met Gly Leu Val Ser Glu Asn Pro Val 1 5 10 15 Thr Val Asp Asp Ala Thr Met Ile Ala Thr Ser Phe Pro Glu Phe Met 20 25 30 Asp Leu Met Ala Gly Leu Gly Ala Lys Ile Glu Leu Ser Asp Thr Lys 35 40 45 Ala Ala 50 <210> 17 <211> 26 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (26) <223> digested peptide fragment by st.aureus V8 protease protease in EPSPS protein <400> 17 Met Ser His Gly Ala Ser Ser Arg Pro Ala Thr Ala Arg Lys Ser Ser 1 5 10 15 Gly Leu Ser Gly Thr Val Arg Ile Pro Gly 20 25 <210> 18 <211> 17 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (17) <223> digestional peptide by st.aureus V8 protease protease in EPSPS protein <400> 18 Val Ile Asn Thr Gly Lys Ala Met Gln Ala Met Gly Ala Arg Ile Arg 1 5 10 15 Lys <210> 19 <211> 18 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (18) <223> digested peptide fragment by st.aureus V8 protease protease in EPSPS protein <400> 19 Phe Gly Asn Ala Ala Thr Gly Cys Arg Leu Thr Met Gly Leu Val Gly 1 5 10 15 Val Tyr <210> 20 <211> 44 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (44) <223> digested peptide fragment by st.aureus V8 protease protease in EPSPS protein <400> 20 Arg Leu Pro Val Thr Leu Arg Gly Pro Lys Thr Pro Thr Pro Ile Thr 1 5 10 15 Tyr Arg Val Pro Met Ala Ser Ala Gln Val Lys Ser Ala Val Leu Leu 20 25 30 Ala Gly Leu Asn Thr Pro Gly Ile Thr Thr Val Ile 35 40 <210> 21 <211> 20 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (20) <223> digested peptide fragment by st.aureus V8 protease protease in EPSPS protein <400> 21 Val Thr Ile Leu Asn Val Leu Met Asn Pro Thr Arg Thr Gly Leu Ile 1 5 10 15 Leu Thr Leu Gln 20 <210> 22 <211> 17 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (17) <223> digested peptide fragment by trypsin and chymotrypsin in EPSPS protein <400> 22 Ile Ile Asp Gly Val Gly Asn Gly Gly Leu Leu Ala Pro Glu Ala Pro 1 5 10 15 Leu <210> 23 <211> 22 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (22) <223> digested peptide fragment by trypsin and chymotrypsin in EPSPS protein <400> 23 Ser Ala Val Leu Leu Ala Gly Leu Asn Thr Pro Gly Ile Thr Thr Val 1 5 10 15 Ile Glu Pro Ile Met Thr 20 <210> 24 <211> 23 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (23) <223> digested peptide fragment by trypsin and chymotrypsin in EPSPS protein <400> 24 Pro Leu Val Ala Ala Leu Leu Val Pro Gly Ser Asp Val Thr Ile Leu 1 5 10 15 Asn Val Leu Met Asn Pro Thr 20 <210> 25 <211> 19 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (19) <223> digested peptide fragment by trypsin and chymotrypsin in EPSPS protein <400> 25 Thr Gly Leu Ile Leu Thr Leu Gln Glu Met Gly Ala Asp Ile Glu Val 1 5 10 15 Ile asn pro <210> 26 <211> 16 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (16) <223> digested peptide fragment by trypsin and chymotrypsin in EPSPS protein <400> 26 Gly Leu Gly Asn Ala Ser Gly Ala Ala Val Ala Thr His Leu Asp His 1 5 10 15 <210> 27 <211> 22 <212> PRT <213> Agrobacterium sp. <220> <221> PEPTIDE (222) (1) .. (22) <223> digested peptide fragment by trypsin and chymotrypsin in EPSPS protein <400> 27 Leu Val Met Gly Leu Val Ser Glu Asn Pro Val Thr Val Asp Asp Ala 1 5 10 15 Thr Met Ile Ala Thr Ser 20 <210> 28 <211> 25 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE (222) (1) .. (22) <223> digested peptide fragment by trypsin in PATprotein <400> 28 Pro Ala Thr Ala Ala Asp Met Ala Ala Val Cys Asp Ile Val Asn His 1 5 10 15 Tyr Ile Glu Thr Ser Thr Val Asn Phe 20 25 <210> 29 <211> 14 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE (222) (1) .. (14) <223> digested peptide fragment by trypsin in PATprotein <400> 29 Thr Glu Pro Gln Thr Pro Gln Glu Trp Ile Asp Asp Leu Glu 1 5 10 <210> 30 <211> 21 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE (222) (1) .. (21) <223> digested peptide fragment by trypsin in PATprotein <400> 30 Tyr Pro Trp Leu Val Ala Glu Val Glu Gly Val Val Ala Gly Ile Ala 1 5 10 15 Tyr Ala Gly Pro Trp 20 <210> 31 <211> 14 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE (222) (1) .. (14) <223> digested peptide fragment by chymotrypsin in PATprotein <400> 31 Val Ser His Arg His Gln Arg Leu Gly Leu Gly Ser Thr Leu 1 5 10 <210> 32 <211> 22 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE (222) (1) .. (22) <223> digested peptide fragment by chymotrypsin in PATprotein <400> 32 Lys Ser Val Val Ala Val Ile Gly Leu Pro Asn Asp Pro Ser Val Arg 1 5 10 15 Leu His Glu Ala Leu Gly 20 <210> 33 <211> 18 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE (222) (1) .. (18) <223> digested peptide fragment by chymotrypsin in PATprotein <400> 33 Gly Val Val Ala Gly Ile Ala Tyr Ala Gly Pro Trp Lys Ala Arg Asn 1 5 10 15 Ala tyr <210> 34 <211> 26 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE (222) (1) .. (26) <223> digested peptide fragment by st.aureus V8 protease in PAT protein <400> 34 Ser Thr Val Tyr Val Ser His Arg His Gln Arg Leu Gly Leu Gly Ser 1 5 10 15 Thr Leu Tyr Thr His Leu Leu Lys Ser Met 20 25 <210> 35 <211> 21 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE (222) (1) .. (21) <223> digested peptide fragment by st.aureus V8 protease in PAT protein <400> 35 Ala Leu Gly Tyr Thr Ala Arg Gly Thr Leu Arg Ala Ala Gly Tyr Lys 1 5 10 15 His Gly Gly Trp His 20 <210> 36 <211> 25 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE (222) (1) .. (25) <223> digested peptide fragment by submaxillarus protease in PAT protein <400> 36 Pro Ala Thr Ala Ala Asp Met Ala Ala Val Cys Asp Ile Val Asn His 1 5 10 15 Tyr Ile Glu Thr Ser Thr Val Asn Phe 20 25 <210> 37 <211> 23 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE (222) (1) .. (23) <223> digested peptide fragment by submaxillarus protease in PAT protein <400> 37 Tyr Pro Trp Leu Val Ala Glu Val Glu Gly Val Val Ala Gly Ile Ala 1 5 10 15 Tyr Ala Gly Pro Trp Lys Ala 20 <210> 38 <211> 30 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE (222) (1) .. (30) <223> digested peptide fragment by submaxillarus protease in PAT protein <400> 38 Thr Leu Tyr Thr His Leu Leu Lys Ser Met Glu Ala Gln Gly Phe Lys 1 5 10 15 Ser Val Val Ala Val Ile Gly Leu Pro Asn Asp Pro Ser Val 20 25 30 <210> 39 <211> 16 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE (222) (1) .. (16) <223> digested peptide fragment by trypsin and chymotrypsin protease in PAT protein <400> 39 Pro Ala Thr Ala Ala Asp Met Ala Ala Val Cys Asp Ile Val Asn His 1 5 10 15 <210> 40 <211> 13 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE (222) (1) .. (13) <223> digested peptide fragment by trypsin and chymotrypsin protease in PAT protein <400> 40 Leu Val Ala Glu Val Glu Gly Val Val Ala Gly Ile Ala 1 5 10 <210> 41 <211> 14 <212> PRT <213> Streptomyces viridochromogenes <220> <221> PEPTIDE (222) (1) .. (14) <223> digested peptide fragment by trypsin and chymotrypsin protease in PAT protein <400> 41 Ser Val Val Ala Val Ile Gly Leu Pro Asn Asp Pro Ser Val 1 5 10 <210> 42 <211> 24 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE (222) (1) .. (24) <223> digested peptide fragment by trypsin in PAT protein <400> 42 Ala Thr Glu Ala Asp Met Pro Ala Val Cys Thr Ile Val Asn His Tyr 1 5 10 15 Ile Glu Thr Ser Thr Val Asn Phe 20 <210> 43 <211> 21 <212> PRT <213> Streptomyces hygroscopicus <400> 43 Tyr Pro Trp Leu Val Ala Glu Val Asp Gly Glu Val Ala Gly Ile Ala 1 5 10 15 Tyr Ala Gly Pro Trp 20 <210> 44 <211> 20 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE (222) (1) .. (20) <223> digested peptide fragment by trypsin in PAT protein <400> 44 His Gly Asn Trp His Asp Val Gly Phe Trp Gln Ile Asp Phe Ser Leu 1 5 10 15 Pro Val Pro Pro 20 <210> 45 <211> 27 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE (222) (1) .. (27) <223> digested peptide fragment by chymotrypsin in PAT protein <400> 45 Met Ser Pro Glu Arg Arg Pro Ala Asp Ile Arg Arg Ala Thr Glu Ala 1 5 10 15 Asp Met Pro Ala Val Cys Thr Ile Val Asn His 20 25 <210> 46 <211> 21 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE (222) (1) .. (21) <223> digested peptide fragment by chymotrypsin in PAT protein <400> 46 Ser Val Val Ala Val Ile Gly Leu Pro Asn Asp Pro Ser Val Arg Met 1 5 10 15 His Glu Ala Leu Gly 20 <210> 47 <211> 26 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE (222) (1) .. (26) <223> digested peptide fragment by st.aureus V8 in PAT protein <400> 47 Ser Thr Val Tyr Val Ser Pro Arg His Gln Arg Thr Gly Leu Gly Ser 1 5 10 15 Thr Leu Tyr Thr His Leu Leu Lys Ser Leu 20 25 <210> 48 <211> 21 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE (222) (1) .. (21) <223> digested peptide fragment by st. aureus V8 protease in PAT protein <400> 48 Ala Leu Gly Tyr Ala Pro Arg Gly Met Leu Arg Ala Ala Gly Phe Lys 1 5 10 15 His Gly Asn Trp His 20 <210> 49 <211> 15 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE (222) (1) .. (15) <223> digested peptide fragment by trypsin and chymotrypsin in PAT protein <400> 49 Ala Thr Glu Ala Asp Met Pro Ala Val Cys Thr Ile Val Asn His 1 5 10 15 <210> 50 <211> 14 <212> PRT <213> Streptomyces hygroscopicus <220> <221> PEPTIDE (222) (1) .. (14) <223> digested peptide fragment by trypsin and chymotrypsin in PAT protein <400> 50 Ser Val Val Ala Val Ile Gly Leu Pro Asn Asp Pro Ser Val 1 5 10 <210> 51 <211> 41 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (41) <223> digested peptide fragment by trypsin in MonBT protein <400> 51 Ile Gln Phe Asn Asp Met Asn Ser Ala Leu Thr Thr Ala Ile Pro Leu 1 5 10 15 Phe Ala Val Gln Asn Tyr Gln Val Pro Leu Leu Ser Val Tyr Val Gln 20 25 30 Ala Ala Asn Leu His Leu Ser Val Leu 35 40 <210> 52 <211> 25 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (25) <223> digested peptide fragment by trypsin in MonBT protein <400> 52 Gly Glu Tyr Tyr Trp Ser Gly His Gln Ile Met Ala Ser Pro Val Gly 1 5 10 15 Phe Ser Gly Ser Asn Gln Ile Gly Leu 20 25 <210> 53 <211> 26 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (26) <223> digested peptide fragment by trypsin in MonBT protein <400> 53 Thr Asp Val Thr Asp Tyr His Ile Asp Gln Val Ser Asn Leu Val Glu 1 5 10 15 Cys Leu Ser Asp Glu Phe Cys Leu Asp Glu 20 25 <210> 54 <211> 29 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (29) <223> digested peptide fragment by trypsin in MonBT protein <400> 54 Cys Ala His His Ser His His Phe Ser Leu Asp Ile Asp Val Gly Cys 1 5 10 15 Thr Asp Leu Asn Glu Asp Leu Gly Val Trp Val Ile Phe 20 25 <210> 55 <211> 25 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (25) <223> digested peptide fragment by chymotrypsin in MonBT protein <400> 55 Arg Gly Ser Ala Gln Gly Ile Glu Gly Ser Ile Arg Ser Pro His Leu 1 5 10 15 Met Asp Ile Leu Asn Ser Ile Thr Ile 20 25 <210> 56 <211> 29 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (29) <223> digested peptide fragment by chymotrypsin in MonBT protein <400> 56 Cys Leu Asp Glu Lys Lys Glu Leu Ser Glu Lys Val Lys His Ala Lys 1 5 10 15 Arg Leu Ser Asp Glu Arg Asn Leu Leu Gln Asp Pro Asn 20 25 <210> 57 <211> 18 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (18) <223> digested peptide fragment by chymotrypsin in MonBT protein <400> 57 Leu Glu Gly Arg Ala Pro Leu Val Gly Glu Ala Leu Ala Arg Gly Gln 1 5 10 15 Glu gly <210> 58 <211> 23 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (23) <223> digested peptide fragment by submaxillarus protease in MonBT protein <400> 58 Glu Leu Thr Leu Thr Val Leu Asp Ile Val Ser Leu Phe Pro Asn Tyr 1 5 10 15 Asp Ser Pro Pro Tyr Pro Ile 20 <210> 59 <211> 64 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (64) <223> digested peptide fragment by submaxillarus protease in MonBT protein <400> 59 Gly Glu Tyr Tyr Trp Ser Gly His Gln Ile Met Ala Ser Pro Val Gly 1 5 10 15 Phe Ser Gly Ser Asn Gln Ile Gly Leu Lys Thr Asp Val Thr Asp Tyr 20 25 30 His Ile Asp Gln Val Ser Asn Leu Val Glu Cys Leu Ser Asp Glu Phe 35 40 45 Cys Leu Asp Glu Lys Lys Glu Leu Ser Glu Lys Val Lys His Ala Lys 50 55 60 <210> 60 <211> 45 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (45) <223> digested peptide fragment by submaxillarus protease in MonBT protein <400> 60 Gly Ser Thr Asp Ile Thr Ile Gln Gly Gly Asp Asp Val Phe Lys Glu 1 5 10 15 Asn Tyr Val Thr Leu Leu Gly Thr Phe Asp Glu Cys Tyr Pro Thr Tyr 20 25 30 Leu Tyr Gln Lys Ile Asp Glu Ser Lys Leu Lys Ala Tyr 35 40 45 <210> 61 <211> 65 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (65) <223> digested peptide fragment by submaxillarus protease in MonBT protein <400> 61 Tyr Asn Ala Lys His Glu Thr Val Asn Val Pro Gly Thr Gly Ser Leu 1 5 10 15 Trp Pro Leu Ser Ala Pro Ser Pro Ile Gly Lys Cys Ala His His Ser 20 25 30 His His Phe Ser Leu Asp Ile Asp Val Gly Cys Thr Asp Leu Asn Glu 35 40 45 Asp Leu Gly Val Trp Val Ile Phe Lys Ile Lys Thr Gln Asp Gly His 50 55 60 Glu 65 <210> 62 <211> 37 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (37) <223> digested peptide fragment by st.aureus protease in MonBT protein <400> 62 Met Asn Ser Ala Leu Thr Thr Ala Ile Pro Leu Phe Ala Val Gln Asn 1 5 10 15 Tyr Gln Val Pro Leu Leu Ser Val Tyr Val Gln Ala Ala Asn Leu His 20 25 30 Leu Ser Val Leu Arg 35 <210> 63 <211> 31 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (31) <223> digested peptide fragment by st.aureus protease in MonBT protein <400> 63 Thr Val Asn Val Pro Gly Thr Gly Ser Leu Trp Pro Leu Ser Ala Pro 1 5 10 15 Ser Pro Ile Gly Lys Cys Ala His His Ser His His Phe Ser Leu 20 25 30 <210> 64 <211> 13 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (13) <223> digested peptide fragment by trypsin and chymotrypsin protease in MonBT protein <400> 64 Asn Asp Met Asn Ser Ala Leu Thr Thr Ala Ile Pro Leu 1 5 10 <210> 65 <211> 13 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (13) <223> digested peptide fragment by trypsin and chymotrypsin protease in MonBT protein <400> 65 His Ile Asp Gln Val Ser Asn Leu Val Glu Cys Leu Ser 1 5 10 <210> 66 <211> 13 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (13) <223> digested peptide fragment by trypsin and chymotrypsin protease in MonBT protein <400> 66 Gly Ser Thr Asp Ile Thr Ile Gln Gly Gly Asp Asp Val 1 5 10 <210> 67 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (17) <223> digested peptide fragment by trypsin and chymotrypsin protease in MonBT protein <400> 67 Ser Leu Asp Ile Asp Val Gly Cys Thr Asp Leu Asn Glu Asp Leu Gly 1 5 10 15 Val <210> 68 <211> 58 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (58) <223> digested peptide fragment by trypsin in cry1 protein <400> 68 Ile Glu Thr Gly Tyr Thr Pro Ile Asp Ile Ser Leu Ser Leu Thr Gln 1 5 10 15 Phe Leu Leu Ser Glu Phe Val Pro Gly Ala Gly Phe Val Leu Gly Leu 20 25 30 Val Asp Ile Ile Trp Gly Ile Phe Gly Pro Ser Gln Trp Asp Ala Phe 35 40 45 Leu Val Gln Ile Glu Gln Leu Ile Asn Gln 50 55 <210> 69 <211> 47 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (47) <223> digested peptide fragment by trypsin in cry1 protein <400> 69 Gly Phe Asn Tyr Trp Ser Gly His Gln Ile Thr Thr Ser Pro Val Gly 1 5 10 15 Phe Ser Gly Pro Glu Phe Ala Phe Pro Leu Phe Gly Asn Ala Gly Asn 20 25 30 Ala Ala Pro Pro Val Leu Val Ser Leu Thr Gly Leu Gly Ile Phe 35 40 45 <210> 70 <211> 34 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (34) <223> digested peptide fragment by trypsin in cry1 protein <400> 70 Ile Ile Leu Gly Ser Gly Pro Asn Asn Gln Glu Leu Phe Val Leu Asp 1 5 10 15 Gly Thr Glu Phe Ser Phe Ala Ser Leu Thr Thr Asn Leu Pro Ser Thr 20 25 30 Ile Tyr <210> 71 <211> 33 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (33) <223> digested peptide fragment by trypsin in cry1 protein <400> 71 Thr Val Gly Phe Thr Thr Pro Phe Asn Phe Ser Asn Gly Ser Ser Val 1 5 10 15 Phe Thr Leu Ser Ala His Val Phe Asn Ser Gly Asn Glu Val Tyr Ile 20 25 30 Asp <210> 72 <211> 26 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (26) <223> digested peptide fragment by trypsin in cry1 protein <400> 72 Thr Asp Gly Thr Asp Tyr His Ile Asp Gln Val Ser Asn Leu Val Glu 1 5 10 15 Cys Leu Ser Asp Glu Phe Cys Leu Asp Glu 20 25 <210> 73 <211> 29 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (29) <223> digested peptide fragment by trypsin in cry1 protein <400> 73 Cys Ala His His Ser His His Phe Ser Leu Asp Ile Asp Val Gly Cys 1 5 10 15 Thr Asp Leu Asn Glu Asp Leu Gly Val Trp Val Ile Phe 20 25 <210> 74 <211> 28 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (28) <223> digested peptide fragment by trypsin in cry1 protein <400> 74 Glu Ser Val Asp Ala Leu Phe Val Asn Ser Gln Tyr Asp Gln Leu Gln 1 5 10 15 Ala Asp Thr Asn Ile Ala Met Ile His Ala Ala Asp 20 25 <210> 75 <211> 23 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (23) <223> digested peptide fragment by trypsin in cry1 protein <400> 75 Glu Ala Tyr Leu Pro Glu Leu Ser Val Ile Pro Gly Val Asn Ala Ala 1 5 10 15 Ile Phe Glu Glu Leu Glu Gly 20 <210> 76 <211> 33 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (33) <223> digested peptide fragment by trypsin in cry1 protein <400> 76 Phe Ser Asn Cys Val Glu Glu Glu Ile Tyr Pro Asn Asn Thr Val Thr 1 5 10 15 Cys Asn Asp Tyr Thr Val Asn Gln Glu Glu Tyr Gly Gly Ala Tyr Thr 20 25 30 Ser <210> 77 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (19) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 77 Gly Asn Ala Gly Asn Ala Ala Pro Pro Val Leu Val Ser Leu Thr Gly 1 5 10 15 Leu Gly Ile <210> 78 <211> 24 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (24) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 78 Arg Gln Arg Gly Thr Val Asp Ser Leu Asp Val Ile Pro Pro Gln Asp 1 5 10 15 Asn Ser Val Pro Pro Arg Ala Gly 20 <210> 79 <211> 21 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (21) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 79 Gln Ile Pro Leu Thr Lys Ser Thr Asn Leu Gly Ser Gly Thr Ser Val 1 5 10 15 Val Lys Gly Pro Gly 20 <210> 80 <211> 28 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (28) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 80 Thr Gly Gly Asp Ile Leu Arg Arg Thr Ser Pro Gly Leu Ile Ser Thr 1 5 10 15 Leu Arg Val Asn Ile Thr Ala Pro Leu Ser Gln Arg 20 25 <210> 81 <211> 15 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (15) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 81 His Ile Asp Gln Val Ser Asn Leu Val Glu Cys Leu Ser Asp Glu 1 5 10 15 <210> 82 <211> 29 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (29) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 82 Cys Leu Asp Glu Lys Gln Glu Leu Ser Glu Lys Val Lys His Ala Lys 1 5 10 15 Arg Leu Ser Asp Glu Arg Asn Leu Leu Gln Asp Pro Asn 20 25 <210> 83 <211> 22 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (22) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 83 Pro Val Ser Ala Pro Lys Pro Ile Gly Lys Cys Gly Glu Pro Asn Arg 1 5 10 15 Cys Ala Pro His Leu Glu 20 <210> 84 <211> 20 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (20) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 84 Asn Pro Asp Leu Asp Cys Ser Cys Arg Asp Gly Glu Lys Cys Ala His 1 5 10 15 His Ser His His 20 <210> 85 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (17) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 85 Ser Leu Asp Ile Asp Val Gly Cys Thr Asp Leu Asn Glu Asp Leu Gly 1 5 10 15 Val <210> 86 <211> 16 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (16) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 86 Asp Gln Leu Gln Ala Asp Thr Asn Ile Ala Met Ile His Ala Ala Asp 1 5 10 15 <210> 87 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (17) <223> digested peptide fragment by chymotrypsin in cry1 protein <400> 87 Gly Glu Gly Cys Val Thr Ile His Glu Ile Glu Asn Asn Thr Asp Glu 1 5 10 15 Leu <210> 88 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (19) <223> digested peptide fragment by trypsin and chymotrypsin in cry1 protein <400> 88 Gly Asn Ala Gly Asn Ala Ala Pro Pro Val Leu Val Ser Leu Thr Gly 1 5 10 15 Leu Gly Ile <210> 89 <211> 18 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (18) <223> digested peptide fragment by trypsin and chymotrypsin in cry1 protein <400> 89 Gly Thr Val Asp Ser Leu Asp Val Ile Pro Pro Gln Asp Asn Ser Val 1 5 10 15 Pro Pro <210> 90 <211> 15 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (15) <223> digested peptide fragment by trypsin and chymotrypsin in cry1 protein <400> 90 His Ile Asp Gln Val Ser Asn Leu Val Glu Cys Leu Ser Asp Glu 1 5 10 15 <210> 91 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (17) <223> digested peptide fragment by trypsin and chymotrypsin and in cry1 protein <400> 91 Ser Leu Asp Ile Asp Val Gly Cys Thr Asp Leu Asn Glu Asp Leu Gly 1 5 10 15 Val <210> 92 <211> 16 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (16) <223> digested peptide fragment by trypsin and chymotrypsin and in cry1 protein <400> 92 Asp Gln Leu Gln Ala Asp Thr Asn Ile Ala Met Ile His Ala Ala Asp 1 5 10 15 <210> 93 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (17) <223> digested peptide fragment by trypsin and chymotrypsin in cry1 protein <400> 93 Gly Glu Gly Cys Val Thr Ile His Glu Ile Glu Asn Asn Thr Asp Glu 1 5 10 15 Leu <210> 94 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (19) <223> digested peptide fragment by trypsin in cryBI protein <400> 94 Thr Asp His Ser Leu Tyr Val Ala Pro Val Val Gly Thr Val Ser Ser 1 5 10 15 Phe leu leu <210> 95 <211> 33 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (33) <223> digested peptide fragment by trypsin in cryBI protein <400> 95 Glu Phe Asn Gln Gln Val Asp Asn Phe Leu Asn Pro Thr Gln Asn Pro 1 5 10 15 Val Pro Leu Ser Ile Thr Ser Ser Val Asn Thr Met Gln Gln Leu Phe 20 25 30 Leu <210> 96 <211> 28 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (28) <223> digested peptide fragment by trypsin in cryBI protein <400> 96 Leu Pro Gln Phe Gln Ile Gln Gly Tyr Gln Leu Leu Leu Leu Pro Leu 1 5 10 15 Phe Ala Gln Ala Ala Asn Met His Leu Ser Phe Ile 20 25 <210> 97 <211> 51 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (51) <223> digested peptide fragment by trypsin in cryBI protein <400> 97 Tyr Gln Ser Leu Met Val Ser Ser Gly Ala Asn Leu Tyr Ala Ser Gly 1 5 10 15 Ser Gly Pro Gln Gln Thr Gln Ser Phe Thr Ala Gln Asn Trp Pro Phe 20 25 30 Leu Tyr Ser Leu Phe Gln Val Asn Ser Asn Tyr Ile Leu Ser Gly Ile 35 40 45 Ser Gly Thr 50 <210> 98 <211> 35 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (35) <223> digested peptide fragment by trypsin in cryBI protein <400> 98 Val Asn Tyr Ser Gly Gly Val Ser Ser Gly Leu Ile Gly Ala Thr Asn 1 5 10 15 Leu Asn His Asn Phe Asn Cys Ser Thr Val Leu Pro Pro Leu Ser Thr 20 25 30 Pro phe val 35 <210> 99 <211> 37 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (37) <223> digested peptide fragment by trypsin in cryBI protein <400> 99 Asn Asn Ile Tyr Ala Ala Asn Glu Asn Gly Thr Met Ile His Leu Ala 1 5 10 15 Pro Glu Asp Tyr Thr Gly Phe Thr Ile Ser Pro Ile His Ala Thr Gln 20 25 30 Val Asn Asn Gln Thr 35 <210> 100 <211> 27 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (27) <223> digested peptide fragment by trypsin in cryBI protein <400> 100 Val Thr Ile Asn Gly Arg Val Tyr Thr Val Ser Asn Val Asn Thr Thr 1 5 10 15 Thr Asn Asn Asp Gly Val Asn Asp Asn Gly Ala 20 25 <210> 101 <211> 47 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (47) <223> digested peptide fragment by trypsin in cryBI protein <400> 101 Phe Ser Asp Ile Asn Ile Gly Asn Ile Val Ala Ser Asp Asn Thr Asn 1 5 10 15 Val Thr Leu Asp Ile Asn Val Thr Leu Asn Ser Gly Thr Pro Phe Asp 20 25 30 Leu Met Asn Ile Met Phe Val Pro Thr Asn Leu Pro Pro Leu Tyr 35 40 45 <210> 102 <211> 22 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (22) <223> digested peptide fragment by trypsin and chymotrypsin in cryBI protein <400> 102 Leu Asn Pro Thr Gln Asn Pro Val Pro Leu Ser Ile Thr Ser Ser Val 1 5 10 15 Asn Thr Met Gln Gln Leu 20 <210> 103 <211> 18 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (18) <223> digested peptide fragment by trypsin and chymotrypsin in cryBI protein <400> 103 Pro Asn Ile Gly Gly Leu Pro Gly Ser Thr Thr Thr Thr His Ser Leu Asn 1 5 10 15 Ser ala <210> 104 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (19) <223> digested peptide fragment by trypsin and chymotrypsin in cryBI protein <400> 104 Thr Val Ser Asn Val Asn Thr Thr Thr Asn Asn Asp Gly Val Asn Asp 1 5 10 15 Asn Gly Ala <210> 105 <211> 29 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (29) <223> digested peptide fragment by trypsin and chymotrypsin in cryBI protein <400> 105 Ser Asp Ile Asn Ile Gly Asn Ile Val Ala Ser Asp Asn Thr Asn Val 1 5 10 15 Thr Leu Asp Ile Asn Val Thr Leu Asn Ser Gly Thr Pro 20 25 <210> 106 <211> 58 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (58) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 106 Ile Glu Thr Gly Tyr Thr Pro Ile Asp Ile Ser Leu Ser Leu Thr Gln 1 5 10 15 Phe Leu Leu Ser Glu Phe Val Pro Gly Ala Gly Phe Val Leu Gly Leu 20 25 30 Val Asp Ile Ile Trp Gly Ile Phe Gly Pro Ser Gln Trp Asp Ala Phe 35 40 45 Leu Val Gln Ile Glu Gln Leu Ile Asn Gln 50 55 <210> 107 <211> 41 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (41) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 107 Ile Gln Phe Asn Asp Met Asn Ser Ala Leu Thr Thr Ala Ile Pro Leu 1 5 10 15 Phe Ala Val Gln Asn Tyr Gln Val Pro Leu Leu Ser Val Tyr Val Gln 20 25 30 Ala Ala Asn Leu His Leu Ser Val Leu 35 40 <210> 108 <211> 32 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (32) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 108 Pro Phe Asn Ile Gly Ile Asn Asn Gln Gln Leu Ser Val Leu Asp Gly 1 5 10 15 Thr Glu Phe Ala Tyr Gly Thr Ser Ser Asn Leu Pro Ser Ala Val Tyr 20 25 30 <210> 109 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (19) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 109 Ser Gly Thr Val Asp Ser Leu Asp Glu Ile Pro Pro Gln Asn Asn Asn 1 5 10 15 Val Pro Pro <210> 110 <211> 33 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (33) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 110 Thr Val Gly Phe Thr Thr Pro Phe Asn Phe Ser Asn Gly Ser Ser Val 1 5 10 15 Phe Thr Leu Ser Ala His Val Phe Asn Ser Gly Asn Glu Val Tyr Ile 20 25 30 Asp <210> 111 <211> 26 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (26) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 111 Thr Asp Val Thr Asp Tyr His Ile Asp Gln Val Ser Asn Leu Val Glu 1 5 10 15 Cys Leu Ser Asp Glu Phe Cys Leu Asp Glu 20 25 <210> 112 <211> 25 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (25) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 112 Ser His His Phe Ser Leu Asp Ile Asp Val Gly Cys Thr Asp Leu Asn 1 5 10 15 Glu Asp Leu Gly Val Trp Val Ile Phe 20 25 <210> 113 <211> 23 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (23) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 113 Glu Ala Tyr Leu Pro Glu Leu Ser Val Ile Pro Gly Val Asn Ala Ala 1 5 10 15 Ile Phe Glu Glu Leu Glu Gly 20 <210> 114 <211> 32 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (32) <223> digested peptide fragment by trypsin in cryHD-1 protein <400> 114 Ser Asn Cys Val Glu Glu Glu Val Tyr Pro Asn Asn Thr Val Thr Cys 1 5 10 15 Asn Asp Tyr Thr Ala Thr Gln Glu Glu Tyr Glu Gly Thr Tyr Thr Ser 20 25 30 <210> 115 <211> 25 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (25) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 115 Arg Gly Ser Ala Gln Gly Ile Glu Gly Ser Ile Arg Ser Pro His Leu 1 5 10 15 Met Asp Ile Leu Asn Ser Ile Thr Ile 20 25 <210> 116 <211> 20 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (20) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 116 Gly Thr Met Gly Asn Ala Ala Pro Gln Gln Arg Ile Val Ala Gln Leu 1 5 10 15 Gly Gln Gly Val 20 <210> 117 <211> 24 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (24) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 117 Arg Lys Ser Gly Thr Val Asp Ser Leu Asp Glu Ile Pro Pro Gln Asn 1 5 10 15 Asn Asn Val Pro Pro Arg Gln Gly 20 <210> 118 <211> 31 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (31) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 118 Asn Asn Ile Ile Pro Ser Ser Gln Ile Thr Gln Ile Pro Leu Thr Lys 1 5 10 15 Ser Thr Asn Leu Gly Ser Gly Thr Ser Val Val Lys Gly Pro Gly 20 25 30 <210> 119 <211> 27 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (27) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 119 Gly Gly Asp Ile Leu Arg Arg Thr Ser Pro Gly Gln Ile Ser Thr Leu 1 5 10 15 Arg Val Asn Ile Thr Ala Pro Leu Ser Gln Arg 20 25 <210> 120 <211> 29 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (29) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 120 Cys Leu Asp Glu Lys Lys Glu Leu Ser Glu Lys Val Lys His Ala Lys 1 5 10 15 Arg Leu Ser Asp Glu Arg Asn Leu Leu Gln Asp Pro Asn 20 25 <210> 121 <211> 23 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (23) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 121 Asp Arg Leu Gln Ala Asp Thr Asn Ile Ala Met Ile His Ala Ala Asp 1 5 10 15 Lys Arg Val His Ser Ile Arg 20 <210> 122 <211> 22 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (22) <223> digested peptide fragment by chymotrypsin in cryHD-1 protein <400> 122 Asn Val Lys Gly His Val Asp Val Glu Glu Gln Asn Asn His Arg Ser 1 5 10 15 Val Leu Val Val Pro Glu 20 <210> 123 <211> 16 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (16) <223> digested peptide fragment by trypsin and chymotrypsin in cryHD-1 protein <400> 123 Asn Ile Gly Ile Asn Asn Gln Gln Leu Ser Val Leu Asp Gly Thr Glu 1 5 10 15 <210> 124 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (19) <223> digested peptide fragment by trypsin and chymotrypsin in cryHD-1 protein <400> 124 Ser Gly Thr Val Asp Ser Leu Asp Glu Ile Pro Pro Gln Asn Asn Asn 1 5 10 15 Val Pro Pro <210> 125 <211> 14 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (14) <223> digested peptide fragment by trypsin and chymotrypsin in cryHD-1 protein <400> 125 Ser Ala Thr Met Ser Ser Gly Ser Asn Leu Gln Ser Gly Ser 1 5 10 <210> 126 <211> 15 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (15) <223> digested peptide fragment by trypsin and chymotrypsin in cryHD-1 protein <400> 126 His Ile Asp Gln Val Ser Asn Leu Val Glu Cys Leu Ser Asp Glu 1 5 10 15 <210> 127 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (17) <223> digested peptide fragment by trypsin and chymotrypsin in cryHD-1 protein <400> 127 Ser Leu Asp Ile Asp Val Gly Cys Thr Asp Leu Asn Glu Asp Leu Gly 1 5 10 15 Val <210> 128 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (17) <223> digested peptide fragment by trypsin and chymotrypsin in cryHD-1 protein <400> 128 Gly Glu Gly Cys Val Thr Ile His Glu Ile Glu Asn Asn Thr Asp Glu 1 5 10 15 Leu <210> 129 <211> 38 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (38) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 129 Gly Ile Ser Val Val Gly Asp Leu Leu Gly Val Val Gly Phe Pro Phe 1 5 10 15 Gly Gly Ala Leu Val Ser Phe Tyr Thr Asn Phe Leu Asn Thr Ile Trp 20 25 30 Pro Ser Glu Asp Pro Trp 35 <210> 130 <211> 21 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (21) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 130 Ala Leu Ala Glu Leu Gln Gly Leu Gln Asn Asn Val Glu Asp Tyr Val 1 5 10 15 Ser Ala Leu Ser Ser 20 <210> 131 <211> 29 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (29) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 131 Asn Ser Met Pro Ser Phe Ala Ile Ser Gly Tyr Glu Val Leu Phe Leu 1 5 10 15 Thr Thr Tyr Ala Gln Ala Ala Asn Thr His Leu Phe Leu 20 25 <210> 132 <211> 21 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (21) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 132 Phe Gln Pro Gly Tyr Tyr Gly Asn Asp Ser Phe Asn Tyr Trp Ser Gly 1 5 10 15 Asn Tyr Val Ser Thr 20 <210> 133 <211> 20 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (20) <223> digested peptide fragment by trypsin in cryIIIA protein <133> 133 Val Glu Phe Ser Gln Tyr Asn Asp Gln Thr Asp Glu Ala Ser Thr Gln 1 5 10 15 Thr Tyr Asp Ser 20 <210> 134 <211> 23 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (23) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 134 Asn Val Gly Ala Val Ser Trp Asp Ser Ile Asp Gln Leu Pro Pro Glu 1 5 10 15 Thr Thr Asp Glu Pro Leu Glu 20 <210> 135 <211> 28 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (28) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 135 Phe Thr Gly Gly Asp Ile Ile Gln Cys Thr Glu Asn Gly Ser Ala Ala 1 5 10 15 Thr Ile Tyr Val Thr Pro Asp Val Ser Tyr Ser Gln 20 25 <210> 136 <211> 26 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (26) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 136 Ile His Tyr Ala Ser Thr Ser Gln Ile Thr Phe Thr Leu Ser Leu Asp 1 5 10 15 Gly Ala Pro Phe Asn Gln Tyr Tyr Phe Asp 20 25 <210> 137 <211> 36 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (36) <223> digested peptide fragment by trypsin in cryIIIA protein <400> 137 Gly Asp Thr Leu Thr Tyr Asn Ser Phe Asn Leu Ala Ser Phe Ser Thr 1 5 10 15 Pro Phe Glu Leu Ser Gly Asn Asn Leu Gln Ile Gly Val Thr Gly Leu 20 25 30 Ser Ala Gly Asp 35 <210> 138 <211> 18 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (18) <223> digested peptide fragment by chymotrypsin in cryIIIA protein <400> 138 Ala Lys Asn Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln Asn Asn Val 1 5 10 15 Glu asp <139> <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (19) <223> digested peptide fragment by chymotrypsin in cryIIIA protein <400> 139 Gln Lys Asn Pro Val Ser Ser Arg Asn Pro His Ser Gln Gly Arg Ile 1 5 10 15 Arg Glu Leu <210> 140 <211> 18 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (18) <223> digested peptide fragment by chymotrypsin in cryIIIA protein <400> 140 Asp Ser Ile Asp Gln Leu Pro Pro Glu Thr Thr Asp Glu Pro Leu Glu 1 5 10 15 Lys gly <210> 141 <211> 20 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (20) <223> digested peptide fragment by chymotrypsin in cryIIIA protein <400> 141 Glu Leu Ser Gly Asn Asn Leu Gln Ile Gly Val Thr Gly Leu Ser Ala 1 5 10 15 Gly asp lys val 20 <210> 142 <211> 28 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (28) <223> digested peptide fragment by submaxillarus protease in cryIIIA protein <400> 142 Leu Leu Gly Val Val Gly Phe Pro Phe Gly Gly Ala Leu Val Ser Phe 1 5 10 15 Tyr Thr Asn Phe Leu Asn Thr Ile Trp Pro Ser Glu 20 25 <210> 143 <211> 67 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (67) <223> digested peptide fragment by submaxillarus protease in cryIIIA protein <400> 143 Tyr Val Ser Ala Leu Ser Ser Trp Gln Lys Asn Pro Val Ser Ser Arg 1 5 10 15 Asn Pro His Ser Gln Gly Arg Ile Arg Glu Leu Phe Ser Gln Ala Glu 20 25 30 Ser His Phe Arg Asn Ser Met Pro Ser Phe Ala Ile Ser Gly Tyr Glu 35 40 45 Val Leu Phe Leu Thr Thr Tyr Ala Gln Ala Ala Asn Thr His Leu Phe 50 55 60 Leu Leu Lys 65 <210> 144 <211> 54 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (54) <223> digested peptide fragment by submaxillarus protease in cryIIIA protein <400> 144 Ile Ile Thr Ser Pro Phe Tyr Gly Asn Lys Ser Ser Glu Pro Val Gln 1 5 10 15 Asn Leu Glu Phe Asn Gly Glu Lys Val Tyr Arg Ala Val Ala Asn Thr 20 25 30 Asn Leu Ala Val Trp Pro Ser Ala Val Tyr Ser Gly Val Thr Lys Val 35 40 45 Glu Phe Ser Gln Tyr Asn 50 <210> 145 <211> 35 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (35) <223> digested peptide fragment by submaxillarus protease in cryIIIA protein <400> 145 Glu Pro Leu Glu Lys Gly Tyr Ser His Gln Leu Asn Tyr Val Met Cys 1 5 10 15 Phe Leu Met Gln Gly Ser Arg Gly Thr Ile Pro Val Leu Thr Trp Thr 20 25 30 His Lys Ser 35 <210> 146 <211> 30 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (30) <223> digested peptide fragment by submaxillarus protease in cryIIIA protein <400> 146 Ser Lys Lys Ile Thr Gln Leu Pro Leu Val Lys Ala Tyr Lys Leu Gln 1 5 10 15 Ser Gly Ala Ser Val Val Ala Gly Pro Arg Phe Thr Gly Gly 20 25 30 <210> 147 <211> 25 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (25) <223> digested peptide fragment by submaxillarus protease in cryIIIA protein <400> 147 Val Ser Tyr Ser Gln Lys Tyr Arg Ala Arg Ile His Tyr Ala Ser Thr 1 5 10 15 Ser Gln Ile Thr Phe Thr Leu Ser Leu 20 25 <210> 148 <211> 33 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (33) <223> digested peptide fragment by submaxillarus protease in cryIIIA protein <400> 148 Thr Leu Thr Tyr Asn Ser Phe Asn Leu Ala Ser Phe Ser Thr Pro Phe 1 5 10 15 Glu Leu Ser Gly Asn Asn Leu Gln Ile Gly Val Thr Gly Leu Ser Ala 20 25 30 Gly <210> 149 <211> 27 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (27) <223> digested peptide fragment by st.aureus V8 protease in cryIIIA protein <400> 149 Leu Leu Gly Val Val Gly Phe Pro Phe Gly Gly Ala Leu Val Ser Phe 1 5 10 15 Tyr Thr Asn Phe Leu Asn Thr Ile Trp Pro Ser 20 25 <210> 150 <211> 25 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (25) <223> digested peptide fragment by st.aureus V8 protease in cryIIIA protein <400> 150 Tyr Val Ser Ala Leu Ser Ser Trp Gln Lys Asn Pro Val Ser Ser Arg 1 5 10 15 Asn Pro His Ser Gln Gly Arg Ile Arg 20 25 <210> 151 <211> 19 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (19) <223> digested peptide fragment by st.aureus V8 protease in cryIIIA protein <400> 151 Val Leu Phe Leu Thr Thr Tyr Ala Gln Ala Ala Asn Thr His Leu Phe 1 5 10 15 Leu Leu Lys <210> 152 <211> 31 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (31) <223> digested peptide fragment by st.aureus V8 protease in cryIIIA protein <400> 152 Lys Gly Tyr Ser His Gln Leu Asn Tyr Val Met Cys Phe Leu Met Gln 1 5 10 15 Gly Ser Arg Gly Thr Ile Pro Val Leu Thr Trp Thr His Lys Ser 20 25 30 <210> 153 <211> 30 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (30) <223> digested peptide fragment by st.aureus V8 protease in cryIIIA protein <400> 153 Ser Lys Lys Ile Thr Gln Leu Pro Leu Val Lys Ala Tyr Lys Leu Gln 1 5 10 15 Ser Gly Ala Ser Val Val Ala Gly Pro Arg Phe Thr Gly Gly 20 25 30 <210> 154 <211> 17 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (17) <223> digested peptide fragment by trypsin and chymotrypsin protease in cryIIIA protein <400> 154 Thr Gly Gly Asp Ile Ile Gln Cys Thr Glu Asn Gly Ser Ala Ala Thr 1 5 10 15 Ile <210> 155 <211> 18 <212> PRT <213> Bacillus thuringiensis <220> <221> PEPTIDE (222) (1) .. (18) <223> digested peptide fragment by trypsin and chymotrypsin protease in cryIIIA protein <400> 155 Glu Leu Ser Gly Asn Asn Leu Gln Ile Gly Val Thr Gly Leu Ser Ala 1 5 10 15 Gly asp

Claims (13)

(a) 유전자재조합식물에 형질전환된 DNA에서 발현되는 재조합단백질의 프로테아제 분해지도(protease cleavage map)를 분석하고;(a) analyzing the protease cleavage map of the recombinant protein expressed in the DNA transformed into the recombinant plant; (b) 상기 분해지도에서 분석한 펩타이들 중 동종의 천연식물 단백질의 프로테아제 분해지도로 제조되는 펩타이드와 상동성을 가지지 않는 일련의 펩타이드를 선택하고;(b) selecting a series of peptides having no homology with the peptides produced by the protease digestion map of the same natural plant protein among the peptides analyzed in the digestion map; (c) 상기의 선택된 펩타이드의 아미노산 서열로 합성펩타이드를 제조하고; 및(c) preparing a synthetic peptide from the amino acid sequence of the peptide selected above; And (d) 상기 합성펩타이드로 항체를 제조하는 것을 특징으로 하는 재조합단백질에 특이적으로 결합하는 항체.(d) an antibody that specifically binds to a recombinant protein, characterized in that the antibody is prepared from the synthetic peptide. 제 1항에 있어서, 상기 형질전환된 DNA는 EPSPS(enolpyru vylshikimate-3-phosphate synthase) DNA인 것을 특징으로 하는 재조합단백질에 특이적으로 결합하는 항체.[Claim 2] The antibody of claim 1, wherein the transformed DNA is EPSPS (enolpyru vylshikimate-3-phosphate synthase) DNA. 제 1항에 있어서, 상기 합성펩타이드는 상기 제 2항의 EPSPS DNA로 발현되는 재조합단백질을 프로테아제로 분해하였을 때 생기는 펩타이드가 염기서열작성기로 작성한 서열번호 1번에서 서열번호 27까지의 펩타이드로 이루어지는 군으로부터 선택되는 것을 특징으로 하는 재조합단백질에 특이적으로 결합하는 항체.According to claim 1, wherein the synthetic peptide is a peptide produced when the recombinant protein expressed in the EPSPS DNA of claim 2 with a protease from the group consisting of peptides SEQ ID NO: 1 to SEQ ID NO: 27 prepared by the nucleotide sequencer An antibody that specifically binds to a recombinant protein, characterized in that selected. 제 1항에 있어서, 상기 형질전환된 DNA는 PAT(Phosphinothricin acetyl transferase) DNA인 것을 특징으로 하는 재조합단백질에 특이적으로 결합하는 항체.According to claim 1, wherein the transformed DNA is an antibody that specifically binds to a recombinant protein, characterized in that the PAT (Phosphinothricin acetyl transferase) DNA. 제 1항에 있어서, 상기 합성펩타이드는 상기 제 4항의 PAT DNA로 발현되는 재조합단백질을 프로테아제로 분해하였을 때 생기는 펩타이드가 염기서열작성기로 작성한 서열번호 28번에서 서열번호 50까지의 펩타이드로 이루어지는 군으로부터 선택되는 것을 특징으로 하는 재조합단백질에 특이적으로 결합하는 항체.According to claim 1, wherein the synthetic peptide is a peptide produced when the recombinant protein expressed by the PAT DNA of claim 4 with a protease from the group consisting of peptides SEQ ID NO: 28 to SEQ ID NO: 50 prepared by the sequencing An antibody that specifically binds to a recombinant protein, characterized in that selected. 제 1항에 있어서, 상기 형질전환된 DNA는 BT(Bacillus thuringiensis) DNA인 것을 특징으로 하는 재조합단백질에 특이적으로 결합하는 항체.[Claim 2] The antibody of claim 1, wherein the transformed DNA is BT ( Bacillus thuringiensis ) DNA. 제 1항에 있어서, 상기 합성펩타이드는 상기 제 6항의 BT DNA로 발현되는 재조합단백질을 프로테아제로 분해하였을 때 생기는 펩타이드가 염기서열작성기로 작성한 서열번호 51번에서 서열번호 155까지의 펩타이드로 이루어지는 군으로부터 선택되는 것을 특징으로 하는 재조합단백질에 특이적으로 결합하는 항체.The method according to claim 1, wherein the synthetic peptide is from the group consisting of the peptides of SEQ ID NO: 51 to SEQ ID NO: 155 prepared by the nucleotide sequencer when the peptide produced when the recombinant protein expressed in the BT DNA of claim 6 with a protease An antibody that specifically binds to a recombinant protein, characterized in that selected. 상기 제 1항의 재조합단백질에 특이적으로 결합하는 항체를 식품에 반응시켜 항원항체반응여부를 확인함으로써 천연식물로 제조한 식품과 유전자재조합식품을 식별하는 것을 특징으로 하는 유전자재조합식품 검사방법.A method for testing genetically modified foods, characterized in that foods made from natural plants and genetically modified foods are identified by reacting the antibodies specifically binding to the recombinant protein of claim 1 to foods to determine whether the antibody reacts with the antigen. 제 8항에 있어서, 상기 식품은 가공식품인 것을 특징으로 하는 유전자재조합식품 검사방법.10. The method of claim 8, wherein the food is a processed food. (a) 검사대상 식품으로부터 단백질을 추출한 단백질추출액;(a) protein extract extracting protein from the food to be tested; (b) 상기 단백질추출액 중의 단백질을 분해하는 효소를 함유하는 효소반응액;(b) an enzyme reaction solution containing an enzyme that degrades the protein in the protein extract; (c) 상기 효소에 의하여 분해된 단백질 중의 재조합단백질과 결합할 수 있는 상기 제 1항의 항체;(c) the antibody of claim 1 capable of binding to a recombinant protein in a protein degraded by the enzyme; (d) 상기 항체가 표면의 소정부분에 묻혀 있는 스트립;(d) a strip in which the antibody is buried in a predetermined portion of the surface; (e) 상기 항체가 재조합단백질과 결합할 때 이를 표시할 수 있는 발색단이 연결된 발색항체; 및 (e) a chromophoric antibody linked to a chromophore that can indicate when the antibody binds to a recombinant protein; And (f) 상기 효소에 의한 단백질 분해가 일어나는 반응기;(f) a reactor in which proteolysis by the enzyme occurs; 를 포함하는 것을 특징으로 하는 유전자재조합식품 검사키트.Genetically modified food test kit comprising a. 제 10항에 있어서, 상기 검사키트는 대조군으로 유전자재조합단백질(EPSPS, BT, PAT를 함유하는 단백질군), 합성펩타이드가 결합된 단백질을 더욱 포함하는 것을 특징으로 하는 유전자재조합식품 검사키트.The test kit according to claim 10, wherein the test kit further comprises a protein recombined protein (EPSPS, BT, PAT-containing protein group), a protein combined with a synthetic peptide. (a) 검사대상 식품으로부터 단백질을 추출한 단백질추출액;(a) protein extract extracting protein from the food to be tested; (b) 상기 단백질추출액 중의 단백질을 분해하는 효소를 함유하는 효소반응액;(b) an enzyme reaction solution containing an enzyme that degrades the protein in the protein extract; (c) 상기 효소에 의하여 분해된 단백질 중의 재조합단백질과 결합할 수 있는 상기 제 1항의 항체;(c) the antibody of claim 1 capable of binding to a recombinant protein in a protein degraded by the enzyme; (d) 상기 항체가 표면에 코팅되어 있는 10-웰 플레이트;(d) a 10-well plate coated with the antibody on the surface; (e) 상기 항체가 재조합단백질과 결합할 때 이를 표시할 수 있는 발색단이 연결된 발색항체; 및 (e) a chromophoric antibody linked to a chromophore that can indicate when the antibody binds to a recombinant protein; And (f) 상기 효소에 의한 단백질 분해가 일어나는 반응기;(f) a reactor in which proteolysis by the enzyme occurs; 를 포함하는 것을 특징으로 하는 유전자재조합식품 검사키트.Genetically modified food test kit comprising a. 제 12항에 있어서, 상기 검사키트는 대조군으로 유전자재조합단백질(EPSPS, BT, PAT를 함유하는 단백질군), 합성펩타이드가 결합된 단백질을 더욱 포함하는 것을 특징으로 하는 유전자재조합식품 검사키트.The test kit according to claim 12, wherein the test kit further comprises a protein recombined protein (EPSPS, BT, PAT-containing protein group), a protein combined with a synthetic peptide.
KR1020000033931A 2000-06-20 2000-06-20 Detection method of genetic recombinant food and detection kit of that KR20050117593A (en)

Priority Applications (4)

Application Number Priority Date Filing Date Title
KR1020000033931A KR20050117593A (en) 2000-06-20 2000-06-20 Detection method of genetic recombinant food and detection kit of that
KR1020010035066A KR20020000127A (en) 2000-06-20 2001-06-20 Detection method of genetically modified organism and detection kit of that
AU2001274652A AU2001274652A1 (en) 2000-06-20 2001-06-20 Detection method of genetic recombinant food and detection kit of that
PCT/KR2001/001054 WO2001098523A2 (en) 2000-06-20 2001-06-20 Detection method of genetic recombinant food and detection kit of that

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
KR1020000033931A KR20050117593A (en) 2000-06-20 2000-06-20 Detection method of genetic recombinant food and detection kit of that

Publications (1)

Publication Number Publication Date
KR20050117593A true KR20050117593A (en) 2005-12-15

Family

ID=19672779

Family Applications (2)

Application Number Title Priority Date Filing Date
KR1020000033931A KR20050117593A (en) 2000-06-20 2000-06-20 Detection method of genetic recombinant food and detection kit of that
KR1020010035066A KR20020000127A (en) 2000-06-20 2001-06-20 Detection method of genetically modified organism and detection kit of that

Family Applications After (1)

Application Number Title Priority Date Filing Date
KR1020010035066A KR20020000127A (en) 2000-06-20 2001-06-20 Detection method of genetically modified organism and detection kit of that

Country Status (1)

Country Link
KR (2) KR20050117593A (en)

Families Citing this family (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
KR100760195B1 (en) * 2004-12-15 2007-09-20 김점순 lock equipment of manhole cover
KR101325912B1 (en) * 2011-01-12 2013-11-07 경희대학교 산학협력단 Polydiacetylene based biosenser

Also Published As

Publication number Publication date
KR20020000127A (en) 2002-01-04

Similar Documents

Publication Publication Date Title
Geisler et al. Molecular aspects of higher plant P-type Ca2+-ATPases
Ortiz-Lopez et al. Amino acid transporters in plants
Waffenschmidt et al. Isodityrosine cross-linking mediates insolubilization of cell walls in Chlamydomonas.
US7883863B2 (en) Apparatuses and methods for determining protease activity
Yoshioka et al. Expression and epitope analysis of the major allergenic protein Fag e 1 from buckwheat
US7714117B2 (en) Biomarkers for toxic algae
Chan et al. Use of two‐dimensional gel electrophoresis to differentiate morphospecies of Alexandrium minutum, a paralytic shellfish poisoning toxin‐producing dinoflagellate of harmful algal blooms
Bieber et al. The complete sequence of the acidic subunit from Mojave toxin determined by Edman degradation and mass spectrometry
KR100381930B1 (en) Method and Primers for Detecting Genetically Modified Organism
KR20050117593A (en) Detection method of genetic recombinant food and detection kit of that
WO2001098523A2 (en) Detection method of genetic recombinant food and detection kit of that
Sokolik et al. The structures of ubiquitin conjugates of yeast Iso-2-cytochrome c
EP2478008A2 (en) Isolated australian coral reef fluorescent proteins and cell-based kinase or phosphatase platforms for cancer drug development
Aitken Purification and Primary Structure of Cytochrome c‐552 from the Cyanobacterium, Synechococcus PCC 6312
US6444457B1 (en) Methods for identifying herbicidal agents that inhibit D1 protease
KR20020077926A (en) Method of assaying lysophospholipase d activity
JP3517712B2 (en) Solid-phase immunoassay for detecting inhibitors of proteolytic enzymes
KR100639393B1 (en) DNA chip for diagnosing living modified plant kit comprising the chip and diagnostic method using the kit
CN109810196A (en) A kind of preparation method and application of rice Cu/Zn-SOD polyclonal antibody
AU2003217221B2 (en) Methods to identify evolutionarily significant changes in polynucleotide and polypeptide sequences in domesticated plants and animals
US20240200085A1 (en) Synthetic activation of multimeric transmembrane receptors
US7439018B2 (en) EG1117 Polynucleotides and uses thereof
CN106699897A (en) Fusion protein used for screening MdmX inhibitor or testing inhibitory activity of MdmX inhibitor
CN106632687A (en) Fusion protein for screening weak MdmX inhibitor or testing inhibition activity of weak MdmX inhibitor
AU2003217221A1 (en) Methods to identify evolutionarily significant changes in polynucleotide and polypeptide sequences in domesticated plants and animals

Legal Events

Date Code Title Description
WITN Withdrawal due to no request for examination