KR100378325B1 - 분자 샤프론을 공동분비시켜 자연적으로 폴딩되고분비되는 단백질을 생산하는 방법 - Google Patents

분자 샤프론을 공동분비시켜 자연적으로 폴딩되고분비되는 단백질을 생산하는 방법 Download PDF

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KR100378325B1
KR100378325B1 KR10-2000-0043241A KR20000043241A KR100378325B1 KR 100378325 B1 KR100378325 B1 KR 100378325B1 KR 20000043241 A KR20000043241 A KR 20000043241A KR 100378325 B1 KR100378325 B1 KR 100378325B1
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polypeptide
protein
periplasm
encoding
dnaj
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KR20010049895A (ko
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암브로시우스도로테
루돌프라이너
샤프너외르크
슈바르츠엘리자베쓰
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에프. 호프만-라 로슈 아게
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    • 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
    • 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
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
    • C12N9/64Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424Serine endopeptidases (3.4.21)
    • C12N9/6456Plasminogen activators
    • C12N9/6459Plasminogen activators t-plasminogen activator (3.4.21.68), i.e. tPA
    • 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
    • C12N1/00Microorganisms; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
    • C12N1/20Bacteria; Culture media therefor
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12PFERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00Preparation of peptides or proteins
    • C12P21/02Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y304/00Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/21Serine endopeptidases (3.4.21)
    • C12Y304/21069Protein C activated (3.4.21.69)
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K2319/00Fusion polypeptide
    • C07K2319/01Fusion polypeptide containing a localisation/targetting motif
    • C07K2319/02Fusion polypeptide containing a localisation/targetting motif containing a signal sequence

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  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Organic Chemistry (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • Genetics & Genomics (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • General Engineering & Computer Science (AREA)
  • Biotechnology (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Biomedical Technology (AREA)
  • Microbiology (AREA)
  • Molecular Biology (AREA)
  • Medicinal Chemistry (AREA)
  • Virology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Tropical Medicine & Parasitology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Physics & Mathematics (AREA)
  • Biophysics (AREA)
  • Plant Pathology (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Peptides Or Proteins (AREA)
  • Enzymes And Modification Thereof (AREA)
KR10-2000-0043241A 1999-07-29 2000-07-27 분자 샤프론을 공동분비시켜 자연적으로 폴딩되고분비되는 단백질을 생산하는 방법 Expired - Lifetime KR100378325B1 (ko)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
EP99114811A EP1077263A1 (de) 1999-07-29 1999-07-29 Verfahren zur Herstellung von natürlich gefalteten und sekretierten Proteinen durch Co-Sekretion von Chaperonen
EP99114811.5 1999-07-29

Publications (2)

Publication Number Publication Date
KR20010049895A KR20010049895A (ko) 2001-06-15
KR100378325B1 true KR100378325B1 (ko) 2003-03-29

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KR10-2000-0043241A Expired - Lifetime KR100378325B1 (ko) 1999-07-29 2000-07-27 분자 샤프론을 공동분비시켜 자연적으로 폴딩되고분비되는 단백질을 생산하는 방법

Country Status (13)

Country Link
US (1) US6455279B1 (https=)
EP (2) EP1077263A1 (https=)
JP (1) JP2001061487A (https=)
KR (1) KR100378325B1 (https=)
CN (1) CN1231595C (https=)
AT (1) ATE299942T1 (https=)
CA (1) CA2313248C (https=)
DE (1) DE60021318T2 (https=)
DK (1) DK1077262T3 (https=)
ES (1) ES2247990T3 (https=)
IN (1) IN190327B (https=)
JO (1) JO2309B1 (https=)
MX (1) MXPA00007339A (https=)

Families Citing this family (39)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
AU6124201A (en) * 2000-05-03 2001-11-12 Expressive Constructs Inc A method and device for improving protein stability and solubility
US6955910B2 (en) 2000-11-14 2005-10-18 Boehringer Ingelheim International Gmbh Method for large scale production of recombinant DNA-derived TPA or K2S molecules
GB0027779D0 (en) * 2000-11-14 2000-12-27 Boehringer Ingelheim Int Methods for large scale production of recombinant dna-derived tpa or k2s molecules
US7087412B2 (en) 2000-11-14 2006-08-08 Boehringer Ingelheim International Gmbh Methods for large scale protein production in prokaryotes
US6979556B2 (en) * 2000-12-14 2005-12-27 Genentech, Inc. Separate-cistron contructs for secretion of aglycosylated antibodies from prokaryotes
US7094757B2 (en) 2001-06-22 2006-08-22 Roche Diagnostics Corporation Complexes comprising a prion protein and a peptidyl prolyl isomerase chaperone, and method for producing and using them
US6962982B2 (en) 2001-06-22 2005-11-08 Roche Diagnostics Corporation Soluble complexes of target proteins and peptidyl prolyl isomerase chaperones and methods of making and using them
DK1402015T3 (da) * 2001-06-22 2011-12-05 Hoffmann La Roche Opløseligt kompleks omfattende et retroviralt overfladeglycoprotein og FkpA eller SlyD
US7094884B2 (en) 2001-06-22 2006-08-22 Roche Diagnostics Corporation Soluble complexes of amylod β peptide and peptidyl prolyl isomerase chaperone and methods of making and using them
KR100441755B1 (ko) * 2001-07-24 2004-08-02 재단법인서울대학교산학협력재단 분자 샤페론을 핵 내부로 이동시키는 방법
KR100968664B1 (ko) * 2001-08-27 2010-07-06 제넨테크, 인크. 항체 발현 및 조립을 위한 시스템
DE10145694A1 (de) * 2001-09-17 2003-04-03 Roche Diagnostics Gmbh Verfahren zur Erhöhung der Löslichkeit, der Expressionsrate und der Aktivität von Proteinen während der rekombinanten Herstellung
WO2004042017A2 (en) * 2002-10-31 2004-05-21 Genentech, Inc. Methods and compositions for increasing antibody production
CA2513113A1 (en) * 2003-01-23 2004-08-05 Genentech, Inc. Methods for producing humanized antibodies and improving yield of antibodies or antigen binding fragments in cell culture
EP1624886A2 (en) * 2003-05-12 2006-02-15 Expressive Constructs, Inc. Methods for increasing cell and tissue viability
AU2004273791A1 (en) * 2003-09-05 2005-03-31 Genentech, Inc. Antibodies with altered effector functions
GB0329681D0 (en) * 2003-12-23 2004-01-28 Delta Biotechnology Ltd Gene expression technique
EP1789446A2 (en) * 2004-09-02 2007-05-30 Genentech, Inc. Heteromultimeric molecules
DK2330200T3 (en) * 2004-12-23 2017-07-24 Albumedix As GENE EXPRESSION TECHNIQUE
DE112005003589T5 (de) * 2005-05-23 2008-04-17 Korea Advanced Institute Of Science & Technology Verfahren zum Herstellen eines Zielproteins unter Verwendung der sHSPs
GB0512707D0 (en) * 2005-06-22 2005-07-27 Delta Biotechnology Ltd Gene expression technique
WO2008067547A2 (en) 2006-11-30 2008-06-05 Research Development Foundation Improved immunoglobulin libraries
CN101294164B (zh) * 2007-04-23 2013-01-16 南京大学 重组人中期因子(rh-Midkine)的表达及其单克隆抗体的制备和应用
AU2008247819B2 (en) 2007-05-01 2013-02-14 Research Development Foundation Immunoglobulin Fc libraries
CN101307310B (zh) * 2007-05-15 2012-08-08 康泰生医科技股份有限公司 具有提高产率及免疫原性的重组蛋白质表达系统
CA2766065C (en) * 2009-06-30 2020-07-21 Research Development Foundation Immunoglobulin fc polypeptides
AU2012214643B2 (en) 2011-02-07 2016-12-15 Research Development Foundation Engineered immunoglobulin Fc polypeptides
WO2014054744A1 (ja) * 2012-10-03 2014-04-10 協和発酵キリン株式会社 培養液にアミノ酸を添加することによるポリペプチドの還元防止方法
JP6345688B2 (ja) 2012-12-05 2018-06-20 ソラ・バイオサイエンシズ・エルエルシー タンパク質発現増強ポリペプチド
JP6724023B2 (ja) 2015-02-09 2020-07-15 リサーチ ディベロップメント ファウンデーション 改善された補体活性化を示す操作された免疫グロブリンfcポリペプチド
CN105296653B (zh) * 2015-11-26 2018-07-06 天津师范大学 采用荧光RT-PCR技术检测周氏啮小蜂Hsp83基因表达的方法
CN105296651B (zh) * 2015-11-26 2018-07-06 天津师范大学 采用荧光RT-PCR技术检测周氏啮小蜂Hsp90基因表达的方法
CN105296652B (zh) * 2015-11-26 2018-07-06 天津师范大学 采用荧光RT-PCR技术检测周氏啮小蜂Hsp40基因表达的方法
CN105296654B (zh) * 2015-11-26 2018-07-06 天津师范大学 采用荧光RT-PCR技术检测周氏啮小蜂Hsp60基因表达的方法
CN110734480B (zh) * 2019-11-07 2021-08-24 中国科学院遗传与发育生物学研究所 大肠杆菌分子伴侣GroEL/ES在协助合成植物Rubisco中的应用
US10973908B1 (en) 2020-05-14 2021-04-13 David Gordon Bermudes Expression of SARS-CoV-2 spike protein receptor binding domain in attenuated salmonella as a vaccine
US12537071B1 (en) 2020-07-22 2026-01-27 David Gordon Bermudes Bacteria having boolean control pathways expressing therapeutic proteins including immunotherapeutic cytotoxins
CN112239760B (zh) * 2020-09-18 2022-02-11 深圳科兴药业有限公司 高效表达重组hGH的重组工程菌及构建方法和应用
CN112940955B (zh) * 2021-04-18 2022-10-18 江南大学 一种高效合成乳铁蛋白的毕赤酵母及其构建方法与应用

Family Cites Families (15)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US4757013A (en) * 1983-07-25 1988-07-12 The Research Foundation Of State University Of New York Cloning vehicles for polypeptide expression in microbial hosts
US5453363A (en) 1985-10-23 1995-09-26 Boehringer Mannheim Gmbh Process for the activation of t-PA or Ing after genetic expression in prokaryotes
DE3537708A1 (de) * 1985-10-23 1987-04-23 Boehringer Mannheim Gmbh Verfahren zur aktivierung von t-pa nach expression in prokaryonten
DE3611817A1 (de) 1986-04-08 1987-10-15 Boehringer Mannheim Gmbh Verfahren zur renaturierung von proteinen
DE68926882T2 (de) * 1988-01-11 1997-02-13 Xoma Corp Plasmidvektor mit pectatlyase-signalsequenz
DE3835350A1 (de) * 1988-10-17 1990-04-19 Boehringer Mannheim Gmbh Aktivierung von gentechnologisch hergestellten, in prokaryonten exprimierten antikoerpern
DE4113750A1 (de) * 1991-04-26 1992-10-29 Boehringer Mannheim Gmbh Verbesserung der renaturierung bei der sekretion von disulfidverbrueckten proteinen
US5789199A (en) * 1994-11-03 1998-08-04 Genentech, Inc. Process for bacterial production of polypeptides
US5639635A (en) * 1994-11-03 1997-06-17 Genentech, Inc. Process for bacterial production of polypeptides
JPH09173078A (ja) * 1995-09-14 1997-07-08 Tadayuki Imanaka 分子シャペロンを用いる蛋白質の製造方法
EP0798380A3 (en) * 1996-03-28 1998-04-29 Mitsui Toatsu Chemicals, Inc. Method for secretory production of protein
US6083715A (en) * 1997-06-09 2000-07-04 Board Of Regents, The University Of Texas System Methods for producing heterologous disulfide bond-containing polypeptides in bacterial cells
JP3344618B2 (ja) * 1997-06-20 2002-11-11 株式会社エイチ・エス・ピー研究所 シャペロン発現プラスミド
EP1048732A1 (de) 1999-04-26 2000-11-02 F. Hoffmann-La Roche Ag Verfahren zur Herstellung von natürlich gefalteten und sekretierten Proteinen
FI109361B (fi) * 1999-05-04 2002-07-15 Korpela Timo Mikrobinen proteiinin ilmentämisjärjestelmä

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US6455279B1 (en) 2002-09-24
CA2313248C (en) 2010-05-25
IN190327B (https=) 2003-07-19
DK1077262T3 (da) 2005-11-07
ES2247990T3 (es) 2006-03-16
CA2313248A1 (en) 2001-01-29
DE60021318D1 (de) 2005-08-25
CN1231595C (zh) 2005-12-14
EP1077262B1 (en) 2005-07-20
KR20010049895A (ko) 2001-06-15
DE60021318T2 (de) 2006-05-24
ATE299942T1 (de) 2005-08-15
MXPA00007339A (es) 2002-08-06
EP1077262A1 (en) 2001-02-21
EP1077263A1 (de) 2001-02-21
JO2309B1 (en) 2005-09-12
JP2001061487A (ja) 2001-03-13
CN1283702A (zh) 2001-02-14

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