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

Abstract

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

Detection method of genetic recombinant food and detection kit of that}

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.

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.

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.

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.

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.

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.

Therefore, there is an urgent need for new technologies for testing GM plants and foods made from GM plants.

Accordingly, an object of the present invention is to provide a method for assaying genetically modified foods.

It is another object of the present invention to provide a test kit capable of assaying genetically modified foods.

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.

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.

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.

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.

Hereinafter, the present invention will be described in detail.

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.

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.

In the present invention, the test method for detecting the EPSPS, PAT and BT recombinant protein was tested.

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.

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.

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.

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.

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.

Certain selected peptides of the invention are shown below.

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.

Protease Selected specific peptide SEQ ID NO: Trypsin EGDTWIIDGVGNGGLLAPEAPLDFGNAATGC One LTGQVIDVPGDPSSTAFPLVAALLVPGSDVTILNVLMNPT 2 APSMIDEYPILAVAAAFAEGATVMNGLEEL 3 IAMSFLVMGLVSENPVTVDDATMIATSFPEFMDLMAGLGA 4 Chymotrypsin GGLASGETRITGLLEGEDVINTGKAMQAMGARIRKEGDT 5 IGDASLTKRPMGRVLNPLREMGVQVKSEHGDRLPVTLRGPKTPTPI 6 VPMASAQVKSAVLLAGLNTPGITTVIEPIMTRDHTEKMLQG 7 GANLTVETDADGVRTIRLEGRGKLTGQVIDVPGDPSSTA 8 LVPGSDVTILNVLMNPTRTGLILTLQEMGADIEVINPRLAGGEDVADLRVRSSTLKGVTVPEDRAPSMIDE 9 AEGATVMNGLEELRVKESDRLSAVANGLKLNGVDCDEGETSLVVRGRPDGKGLGNASGAAVATHLDHRIAMS 10 Supmacilarus KEGDTWIIDGVGNGGLLAPEAPLDFGNAATGC 11 VPMASAQVKSAVLLAGLNTPGITTVIEPIMT 12 GKLTGQVIDVPGDPSSTAFPLVAALLVPGSDVTILNVLMNPT 13 APSMIDEYPILAVAAAFAEGATVMNGLEEL 14 LSAVANGLKLNGVDCDEGETSLVV 15 IAMSFLVMGLVSENPVTVDDATMIATSFPEFMDLMAGLGAKIELSDTKAA 16 St. Aureus V8 MSHGASSRPATARKSSGLSGTVRIPG 17 VINTGKAMQAMGARIRK 18 FGNAATGCRLTMGLVGVY 19 RLPVTLRGPKTPTPITYRVPMASAQVKSAVLLAGLNTPGITTVI 20 VTILNVLMNPTRTGLILTLQ 21 Trypsin + chymotrypsin IIDGVGNGGLLAPEAPLD 22 SAVLLAGLNTPGITTVIEPIMT 23 PLVAALLVPGSDVTILNVLMNPT 24 TGLILTLQEMGADIEVINP 25 GLGNASGAAVATHLDH 26 LVMGLVSENPVTVDDATMIATS 27

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.

Treated Protease Selected Specific Peptide Sequence SEQ ID NO: PAT1 (streptomyces viridochromine) Trypsin PATAADMAAVCDIVNHYIETSTVNF 28 TEPQTPQEWIDDLE 29 YPWLVAEVEGVVAGIAYAGPW 30 Chymotrypsin VSHRHQRLGLGSTL 31 KSVVAVIGLPNDPSVRLHEALG 32 St. Aureus V8 GVVAGIAYAGPWKARNAY 33 STVYVSHRHQRLGLGSTLYTHLLKSM 34 ALGYTARGTLRAAGYKHGGWH 35 Supmacilarus PATAADMAAVCDIVNHYIETSTVNF 36 YPWLVAEVEGVVAGIAYAGPWKA 37 TLYTHLLKSMEAQGFKSVVAVIGLPNDPSV 38 Trypsin + chymotrypsin PATAADMAAVCDIVNH 39 LVAEVEGVVAGIA 40 SVVAVIGLPNDPSV 41 PAT2 (Streptomyces hygroscopic picus) Trypsin ATEADMPAVCTIVNHYIETSTVNF 42 YPWLVAEVDGEVAGIAYAGPW 43 HGNWHDV GFWQIDFSLPVPP 44 Chymotrypsin MSPERRPADIRRATEADMPAVCTIVNH 45 SVVAVIGLPNDPSVRMHEALG 46 St. Aureus V8 STVYVSPRHQRTGLGSTLYTHLLKSL 47 ALGYAPRGMLRAAGFKHGNWH 48 Trypsin + chymotrypsin ATEADMPAVCTIVNH 49 SVVAVIGLPNDPSV 50

 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.

gene Protease  Selected Specific Peptide Sequence SEQ ID NO: BT-1 (MonBT) Trypsin IQFNDMNSALTTAIPLFAVQNYQVPLLSVYVQAANLHLSVL 51 GEYYWSGHQIMASPVGFSGSNQIGL 52 TDVTDYHIDQVSNLVECLSDEFCLDE 53 CAHHSHHFSLDIDVGCTDLNEDLGVWVIF 54 Chymotrypsin RGSAQGIEGSIRSPHLMDILNSITI 55 CLDEKKELSEKVKHAKRLSDERNLLQDPN 56 LEGRAPLVGEALARGQEG 57 Supmacilarus ELTLTVLDIVSLFPNYDSPPYPI 58 GEYYWSGHQIMASPVGFSGSNQIGLKTDVTDYHIDQVSNLVECLSDEFCLDEKKELSEKVKHAK 59 GSTDITIQGGDDVFKENYVTLLGTFDECYPTYLYQKIDESKLKAY 60 YNAKHETVNVPGTGSLWPLSAPSPIGKCAHHSHHFSLDIDVGCTDLNEDLGVWVIFKIKTQDGHE 61 St. Aureus V8 MNSALTTAIPLFAVQNYQVPLLSVYVQAANLHLSVLR 62 TVNVPGTGSLWPLSAPSPIGKCAHHSHHFSL 63 Trypsin + Chymotrypsin NDMNSALTTAIPL 64 HIDQVSNLVECLS 65 GSTDITIQGGDDV 66 SLDIDVGCTDLNEDLGV 67 BT-2 Trypsin IETGYTPIDISLSLTQFLLSEFVPGAGFVLGLVDIIWGIFGPSQWDAFLVQIEQLINQ 68 GFNYWSGHQITTSPVGFSGPEFAFPLFGNAGNAAPPVLVSLTGLGIF 69 IILGSGPNNQELFVLDGTEFSFASLTTNLPSTIY 70 TVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYID 71 TDGTDYHIDQVSNLVECLSDEFCLDE 72 CAHHSHHFSLDIDVGCTDLNEDLGVWVIF 73 ESVDALFVNSQYDQLQADTNIAMIHAAD 74 EAYLPELSVIPGVNAAIFEELEG 75  FSNCVEEEIYPNNTVTCNDYTVNQEEYGGAYTS 76 Chymotrypsin  GNAGNAAPPVLVSLTGLGI 77  RQRGTVDSLDVIPPQDNSVPPRAG 78  QIPLTKSTNLGSGTSVVKGPG 79  TGGDILRRTSPGLISTLRVNITAPLSQR 80  HIDQVSNLVECLSDE 81  CLDEKQELSEKVKHAKRLSDERNLLQDPN 82  PVSAPKPIGKCGEPNRCAPHLE 83  NPDLDCSCRDGEKCAHHSHH 84

BT-2 Chymotrypsin SLDIDVGCTDLNEDLGV 85 DQLQADTNIAMIHAAD 86 GEGCVTIHEIENNTDEL 87 Trypsin + chymotrypsin GNAGNAAPPVLVSLTGLGI 88 GTVDSLDVIPPQDNSVPP 89 HIDQVSNLVECLSDE 90 SLDIDVGCTDLNEDLGV 91 DQLQADTNIAMIHAAD 92 GEGCVTIHEIENNTDEL 93 BT-3 (Cry-BI) Trypsin TDHSLYVAPVVGTVSSFLL 94 EFNQQVDNFLNPTQNPVPLSITSSVNTMQQLFL 95 LPQFQIQGYQLLLLPLFAQAANMHLSFI 96 YQSLMVSSGANLYASGSGPQQTQSFTAQNWPFLYSLFQVNSNYILSG ISGT 97 VNYSGGVSSGLIGATNLNHNFNCSTVLPPLSTPFV 98 NNIYAANENGTMIHLAPEDYTGFTISPIHATQVNNQT 99 VTINGRVYTVSNVNTTTNNDGVNDNGA 100 FSDINIGNIVASDNTNVTLDINVTLNSGTPFDLMNIMFVPTNLPPLY 101 Trypsin + chymotrypsin LNPTQNPVPLSITSSVNTMQQL 102 PNIGGLPGSTTTHSLNSA 103 TVSNVNTTTNNDGVNDNGA 104 SDINIGNIVASDNTNVTLDINVTLNSGTP 105 BT-4 (CryHD-1) Trypsin IETGYTPIDISLSLTQFLLSEFVPGAGFVLGLVDIIWGIFGPSQWDAFLVQIEQLINQ 106 IQFNDMNSALTTAIPLFAVQNYQVPLLSVYVQAANLHLSVL 107 PFNIGINNQQLSVLDGTEFAYGTSSNLPSAVY 108 SGTVDSLDEIPPQNNNVPP 109 TVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYID 110 TDVTDYHIDQVSNLVECLSDEFCLDE 111 SHHFSLDIDVGCTDLNEDLGVWVIF 112 EAYLPELSVIPGVNAAIFEELEG 113 SNCVEEEVYPNNTVTCNDYTATQEEYEGTYTS 114 Chymotrypsin RGSAQGIEGSIRSPHLMDILNSITI 115 GTMGNAAPQQRIVAQLGQGV 116 RKSGTVDSLDEIPPQNNNVPPRQG 117  NNIIPSSQITQIPLTKSTNLGSGTSVVKGPG 118  GGDILRRTSPGQISTLRVNITAPLSQR 119  CLDEKKELSEKVKHAKRLSDERNLLQDPN 120  DRLQADTNIAMIHAADKRVHSIR 121  NVKGHVDVEEQNNHRSVLVVPE 122 Trypsin + chymotrypsin  NIGINNQQLSVLDGTE 123  SGTVDSLDEIPPQNNNVPP 124  SATMSSGSNLQSGS 125  HIDQVSNLVECLSDE 126 SLDIDVGCTDLNEDLGV 127

BT-4  GEGCVTIHEIENNTDEL 128 BT-5 (CryIIIA) Trypsin GISVVGDLLGVVGFPFGGALVSFYTNFLNTIWPSEDPW 129 ALAELQGLQNNVEDYVSALSS 130 NSMPSFAISGYEVLFLTTYAQAANTHLFL 131 FQPGYYGNDSFNYWSGNYVST 132 VEFSQYNDQTDEASTQTYDS 133 NVGAVSWDSIDQLPPETTDEPLE 134 FTGGDIIQCTENGSAATIYVTPDVSYSQ 135 IHYASTSQITFTLSLDGAPFNQYYFD 136 GDTLTYNSFNLASFSTPFELSGNNLQIGVTGLSAGD 137 Chymotrypsin AKNKALAELQGLQNNVED 138 QKNPVSSRNPHSQGRIREL 139 DSIDQLPPETTDEPLEKG 140 ELSGNNLQIGVTGLSAGDKV 141 Supmacilarus LLGVVGFPFGGALVSFYTNFLNTIWPSE 142 YVSALSSWQKNPVSSRNPHSQGRIRELFSQAESHFRNSMPSFAISGYEVLFLTTYAQAANTHLFLLK 143 IITSPFYGNKSSEPVQNLEFNGEKVYRAVANTNLAVWPSAVYSGVTKVEFSQYN 144 EPLEKGYSHQLNYVMCFLMQGSRGTIPVLTWTHKSV 145 SKKITQLPLVKAYKLQSGASVVAGPRFTGG 146 VSYSQKYRARIHYASTSQITFTLSL 147 TLTYNSFNLASFSTPFELSGNNLQIGVTGLSAG 148 St. Aureus V8 LLGVVGFPFGGALVSFYTNFLNTIWPS 149 YVSALSSWQKNPVSSRNPHSQGRIR 150 VLFLTTYAQAANTHLFLLK 151 KGYSHQLNYVMCFLMQGSRGTIPVLTWTHKS 152 SKKITQLPLVKAYKLQSGASVVAGPRFTGG 153 Trypsin + chymotrypsin TGGDIIQCTENGSAATI 154 ELSGNNLQIGVTGLSAGD 155

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.

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.

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.

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.

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.

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.

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.

The test kit for genetically modified foods of the present invention further includes other buffer solutions, in addition to the essential components described above.

 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.

Example 1 EPSPS Test

Amino Acid Sequencing of EPSPS

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.

One I-I-D-G-V-G-N-G-G-L-L-A-P-E-A-P-L-D 2 S-A-V-L-L-A-G-L-N-T-P-G-L-T-T-V-I-E-P-I-M-T 3 P-L-V-A-A-L-L-V-P-G-S-D-V-T-I-L-N-V-L-M-N-P-T 4 T-G-L-I-L-T-L-Q-E-M-G-A-D-I-E-V-I-N-P 5 L-V-M-G-L-V-S-E-N-P-V-T-V-D-D-A-T-M-I-A-T-S

Peptide Synthesis

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.

Antibody Production

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.

Experimental Example 1 genetic recombination test of food

(1) soft food

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) hard food

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.

Example 2 PAT inspection

Amino Acid Sequencing of PAT

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.

Example 3 BT Inspection

Amino Acid Sequencing of BT

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.

Example 4 Strip Inspection Kit

 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.

Experimental Example 2

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.

Example 5 ELISA Test Kit

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.

Experimental Example 3

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.

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 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) analyzing the protease cleavage map of the recombinant protein expressed in the DNA transformed into the recombinant plant; (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) preparing a synthetic peptide from the amino acid sequence of the peptide selected above; And (d) an antibody that specifically binds to a recombinant protein, characterized in that the antibody is prepared from the synthetic peptide. [Claim 2] The antibody of claim 1, wherein the transformed DNA is EPSPS (enolpyru vylshikimate-3-phosphate synthase) DNA. 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. 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. 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. [Claim 2] The antibody of claim 1, wherein the transformed DNA is BT ( Bacillus thuringiensis ) DNA. 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. 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. 10. The method of claim 8, wherein the food is a processed food. (a) protein extract extracting protein from the food to be tested; (b) an enzyme reaction solution containing an enzyme that degrades the protein in the protein extract; (c) the antibody of claim 1 capable of binding to a recombinant protein in a protein degraded by the enzyme; (d) a strip in which the antibody is buried in a predetermined portion of the surface; (e) a chromophoric antibody linked to a chromophore that can indicate when the antibody binds to a recombinant protein; And (f) a reactor in which proteolysis by the enzyme occurs; Genetically modified food test kit comprising a. 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) protein extract extracting protein from the food to be tested; (b) an enzyme reaction solution containing an enzyme that degrades the protein in the protein extract; (c) the antibody of claim 1 capable of binding to a recombinant protein in a protein degraded by the enzyme; (d) a 10-well plate coated with the antibody on the surface; (e) a chromophoric antibody linked to a chromophore that can indicate when the antibody binds to a recombinant protein; And (f) a reactor in which proteolysis by the enzyme occurs; Genetically modified food test kit comprising a. 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.