AU4132189A - Process for the activation of genetically engineered, heterologous, disulphide bridge-containing eukaryotic proteins after expression in prokaryotes - Google Patents
Process for the activation of genetically engineered, heterologous, disulphide bridge-containing eukaryotic proteins after expression in prokaryotesInfo
- Publication number
- AU4132189A AU4132189A AU41321/89A AU4132189A AU4132189A AU 4132189 A AU4132189 A AU 4132189A AU 41321/89 A AU41321/89 A AU 41321/89A AU 4132189 A AU4132189 A AU 4132189A AU 4132189 A AU4132189 A AU 4132189A
- Authority
- AU
- Australia
- Prior art keywords
- pref
- expression
- esp
- prokaryotes
- heterologous
- Prior art date
- Legal status (The legal status 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 status listed.)
- Granted
Links
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6456—Plasminogen activators
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6456—Plasminogen activators
- C12N9/6459—Plasminogen activators t-plasminogen activator (3.4.21.68), i.e. tPA
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
- C07K1/1133—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure by redox-reactions involving cystein/cystin side chains
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/555—Interferons [IFN]
- C07K14/565—IFN-beta
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
- C12Y304/21069—Protein C activated (3.4.21.69)
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Wood Science & Technology (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Microbiology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- General Chemical & Material Sciences (AREA)
- Analytical Chemistry (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Mechanical Treatment Of Semiconductor (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
- Lubricants (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
Abstract
Method for activating non-glycosylated tissue plasminogen activator (t-PA) after its expression in prokaryotic cells comprises cell lysis; solubilisation under denaturing and reducing conditions, and reactivation under oxidising conditions in presence of reduced and oxidised glutathione (G5H, G55G). The new feature is that in the last stage is at pH 9-12 (pref. 9.5-11) with G5H and G55G concns. 0.1-20, pref. 0.2-10, mM and 0.01-3, pref. 0.5-1, mM, respectively, and with a non-denaturing concn. of the denaturing agent. Esp. the method is applied to t-PA expressed in E.coli and P. putida. The denaturing agent is pref. arginine, guanidine hydrochloride (both at 0.1-1, esp. 0.25-0.75, mM) or urea, at 0.5-4 (esp. 1-3.5) M in the last stage.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
DE19853537708 DE3537708A1 (en) | 1985-10-23 | 1985-10-23 | METHOD FOR ACTIVATING T-PA AFTER EXPRESSION IN PROKARYONTS |
DE3537708 | 1985-10-23 |
Related Parent Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
AU65993/86A Division AU590029B2 (en) | 1985-10-23 | 1986-10-23 | Process for the activation of genetically engineered, heterologous disulfide bridge-containing eukaryotic proteins after expression in |
Publications (2)
Publication Number | Publication Date |
---|---|
AU4132189A true AU4132189A (en) | 1990-01-04 |
AU607083B2 AU607083B2 (en) | 1991-02-21 |
Family
ID=6284269
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
AU65993/86A Ceased AU590029B2 (en) | 1985-10-23 | 1986-10-23 | Process for the activation of genetically engineered, heterologous disulfide bridge-containing eukaryotic proteins after expression in |
AU41321/89A Expired AU607083B2 (en) | 1985-10-23 | 1989-09-13 | Process for the activation of genetically engineered, heterologous, disulphide bridge-containing eukaryotic proteins after expression in prokaryotes |
Family Applications Before (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
AU65993/86A Ceased AU590029B2 (en) | 1985-10-23 | 1986-10-23 | Process for the activation of genetically engineered, heterologous disulfide bridge-containing eukaryotic proteins after expression in |
Country Status (26)
Country | Link |
---|---|
EP (3) | EP0219874B1 (en) |
JP (2) | JPH0728745B2 (en) |
KR (1) | KR900009139B1 (en) |
AT (2) | ATE98648T1 (en) |
AU (2) | AU590029B2 (en) |
CA (1) | CA1329157C (en) |
CZ (1) | CZ280727B6 (en) |
DD (1) | DD260517A5 (en) |
DE (3) | DE3537708A1 (en) |
DK (2) | DK175091B1 (en) |
ES (2) | ES2061434T3 (en) |
FI (2) | FI94050C (en) |
GR (2) | GR920300062T1 (en) |
HK (2) | HK153596A (en) |
HR (1) | HRP921075B1 (en) |
HU (2) | HUT43643A (en) |
IE (1) | IE62634B1 (en) |
IL (1) | IL80325A (en) |
PT (1) | PT83609B (en) |
SI (1) | SI8611796B (en) |
SK (1) | SK278317B6 (en) |
SU (1) | SU1607689A3 (en) |
UA (1) | UA6023A1 (en) |
WO (1) | WO1987002673A2 (en) |
YU (1) | YU47185B (en) |
ZA (1) | ZA868012B (en) |
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
AU609645B2 (en) * | 1988-10-17 | 1991-05-02 | Boehringer Mannheim Gmbh | Process for the activation of gene-technologically produced, biologically-active proteins expressed in prokaryotes |
WO1992004382A1 (en) * | 1990-09-05 | 1992-03-19 | Bunge (Australia) Pty. Ltd. | Solubilization of proteins in active forms |
Families Citing this family (41)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4766205A (en) * | 1985-11-13 | 1988-08-23 | Beatrice Companies, Inc. | Method for isolation of recombinant polypeptides in biologically active forms |
JP2581668B2 (en) * | 1985-11-27 | 1997-02-12 | 三井東圧化学株式会社 | Novel DNA sequence encoding human tissue plasminogen activator derived from normal human cells and vectors and cells containing the same |
US4777043A (en) * | 1985-12-17 | 1988-10-11 | Genentech, Inc. | Stabilized human tissue plasminogen activator compositions |
AU621051B2 (en) * | 1987-04-28 | 1992-03-05 | Amgen, Inc. | Method for purifying granulocyte-macrophage colony stimulating factor |
DE3722082A1 (en) * | 1987-07-03 | 1989-01-12 | Behringwerke Ag | METHOD FOR DETERMINING THE ACTIVITY OF SERINE PROTEASES OR SERINE PROTEASE INHIBITORS |
CA1340586C (en) * | 1988-09-23 | 1999-06-08 | Cetus Corporation | Process for recovering microbially produced interferon-beta |
DE3832898A1 (en) * | 1988-09-28 | 1990-04-12 | Boehringer Mannheim Gmbh | PRAEPARATE OF EXPRESSED PLASMINOGEN ACTIVATOR IN PROKARYONS |
DE3903581A1 (en) * | 1989-02-07 | 1990-08-16 | Boehringer Mannheim Gmbh | FABRIC PLASMINOGEN ACTIVATOR DERIVATIVE |
DE3942143A1 (en) * | 1989-12-20 | 1991-06-27 | Boehringer Mannheim Gmbh | T-PA PRO STABILIZATION |
EP0545999B1 (en) * | 1990-08-20 | 1997-06-04 | Novo Nordisk A/S | Process for the preparation of biologically active IGF-1 using IGF-1 having an amino-terminal extension |
DE4037196A1 (en) * | 1990-11-22 | 1992-05-27 | Boehringer Mannheim Gmbh | METHOD FOR REACTIVATING DENATURED PROTEIN |
DE4113750A1 (en) | 1991-04-26 | 1992-10-29 | Boehringer Mannheim Gmbh | IMPROVEMENT OF RENATURATION IN THE SECRETION OF DISULFID-BRIDGED PROTEINS |
DE4139000A1 (en) * | 1991-11-27 | 1993-06-03 | Boehringer Mannheim Gmbh | METHOD OF GENERATING BIOLOGICALLY ACTIVE SS-NGF |
US5212091A (en) * | 1992-03-02 | 1993-05-18 | Monsanto Company | Method of producing tissue factor pathway inhibitor |
AU3812993A (en) * | 1992-03-24 | 1993-10-21 | Synergen, Inc. | Refolding and purification of insulin-like growth factor I |
DK0600372T3 (en) | 1992-12-02 | 1997-08-11 | Hoechst Ag | Process for the preparation of proinsulin with properly connected cystine bridges. |
DE4405179A1 (en) * | 1994-02-18 | 1995-08-24 | Hoechst Ag | Method of obtaining insulin with correctly connected cystine bridges |
FR2729972B1 (en) * | 1995-01-31 | 1997-04-18 | Sanofi Sa | PROCESS FOR THE EXTRACTION OF PERIPLASMIC PROTEINS FROM PROKARYOTIC MICROORGANISMS IN THE PRESENCE OF ARGININ |
US5714371A (en) * | 1995-05-12 | 1998-02-03 | Schering Corporation | Method for refolding insoluble aggregates of hepatitis C virus protease |
US5728804A (en) * | 1995-06-02 | 1998-03-17 | Research Corporation Technologies, Inc. | Use of cyclodextrins for protein renaturation |
EP0904355B1 (en) * | 1996-06-11 | 2004-03-03 | Boehringer Mannheim Gmbh | Method of activating denatured protein |
US7153943B2 (en) | 1997-07-14 | 2006-12-26 | Bolder Biotechnology, Inc. | Derivatives of growth hormone and related proteins, and methods of use thereof |
US6653098B1 (en) * | 1998-02-23 | 2003-11-25 | G. D. Searle & Co. | Method of producing mouse and human endostatin |
DE19850429A1 (en) * | 1998-10-27 | 2000-05-04 | Andre Schrattenholz | Fragments |
EP1048732A1 (en) * | 1999-04-26 | 2000-11-02 | F. Hoffmann-La Roche Ag | Process for producing natural folded and secreted proteins |
EP1077263A1 (en) * | 1999-07-29 | 2001-02-21 | F.Hoffmann-La Roche Ag | Process for producing natural folded and secreted proteins by co-secretion of chaperones |
IL152804A0 (en) | 2000-05-16 | 2003-06-24 | Bolder Biotechnology Inc | Methods for refolding proteins containing free cysteine residues |
DE10105911A1 (en) | 2001-02-09 | 2002-08-14 | Roche Diagnostics Gmbh | Expression of the recombinant proteinase K from Tritirachium album in yeast |
DE10105912A1 (en) * | 2001-02-09 | 2002-08-14 | Roche Diagnostics Gmbh | Recombinant Proteinase K |
DE102005033250A1 (en) | 2005-07-15 | 2007-01-18 | Bioceuticals Arzneimittel Ag | Process for purifying G-CSF |
DE202006020194U1 (en) | 2006-03-01 | 2007-12-06 | Bioceuticals Arzneimittel Ag | G-CSF liquid formulation |
TWI476207B (en) | 2006-07-14 | 2015-03-11 | Genentech Inc | Refolding of recombinant proteins |
WO2008076933A2 (en) | 2006-12-14 | 2008-06-26 | Bolder Biotechnology, Inc. | Long acting proteins and peptides and methods of making and using the same |
WO2011113601A1 (en) | 2010-03-17 | 2011-09-22 | Biogenerix Ag | Method for obtaining biologically active recombinant human g-csf |
US20130273607A1 (en) * | 2010-10-20 | 2013-10-17 | Medimmune, Llc | Methods for processing inclusion bodies |
HUP1200171A1 (en) | 2012-03-19 | 2013-09-30 | Richter Gedeon Nyrt | Methods for the production of polypeptides |
HUP1200172A2 (en) | 2012-03-19 | 2013-10-28 | Richter Gedeon Nyrt | Methods for refolding g-csf from inclusion bodies |
CN103852527B (en) * | 2012-12-05 | 2015-05-13 | 中国科学院大连化学物理研究所 | High-flux protein sample pre-treatment device |
US10457716B2 (en) | 2014-08-06 | 2019-10-29 | University Of Notre Dame Du Lac | Protein folding and methods of using same |
WO2018121703A1 (en) | 2016-12-30 | 2018-07-05 | Biogend Therapeutics Co., Ltd. | Recombinant polypeptides, compositions, and methods thereof |
EP4263568A1 (en) | 2020-12-18 | 2023-10-25 | Richter Gedeon Nyrt. | Methods for the purification of refolded fc-peptide fusion protein |
Family Cites Families (12)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS5135481A (en) * | 1974-09-18 | 1976-03-25 | Fujiwa Kako Kk | KOJUNDOHITOROKINAAZE NO SEIHO |
US4468633A (en) | 1982-04-28 | 1984-08-28 | The Bendix Corporation | Adjustable microwave power combiner for a plurality of coaxially mounted impatt diodes |
IL68561A (en) | 1982-05-05 | 1991-01-31 | Genentech Inc | Preparation of polypeptide with human tissue plasminogen activator function,processes for making it,and dna and transformed cell intermediates thereof |
US4432895A (en) * | 1982-11-24 | 1984-02-21 | Hoffmann-La Roche Inc. | Monomeric interferons |
GR79124B (en) * | 1982-12-22 | 1984-10-02 | Genentech Inc | |
GB2138004B (en) * | 1983-03-25 | 1987-05-13 | Celltech Ltd | A process for the production of a protein |
JPS6051119A (en) * | 1983-08-30 | 1985-03-22 | Green Cross Corp:The | Dried pharmaceutical preparation of urokinase |
US4530787A (en) * | 1984-03-28 | 1985-07-23 | Cetus Corporation | Controlled oxidation of microbially produced cysteine-containing proteins |
US4748234A (en) * | 1985-06-26 | 1988-05-31 | Cetus Corporation | Process for recovering refractile bodies containing heterologous proteins from microbial hosts |
US4766205A (en) * | 1985-11-13 | 1988-08-23 | Beatrice Companies, Inc. | Method for isolation of recombinant polypeptides in biologically active forms |
FR2596360B1 (en) * | 1986-04-01 | 1989-02-17 | Sotralentz Sa | CONTAINER ON PALLET WITH FOLDED AND REINFORCED MESH PROTECTION DEVICE |
JPH0651119A (en) * | 1992-07-28 | 1994-02-25 | Sekisui Chem Co Ltd | Production of phase difference plate |
-
1985
- 1985-10-23 DE DE19853537708 patent/DE3537708A1/en active Granted
-
1986
- 1986-10-10 IE IE268386A patent/IE62634B1/en not_active IP Right Cessation
- 1986-10-15 IL IL80325A patent/IL80325A/en not_active IP Right Cessation
- 1986-10-17 SK SK7526-86A patent/SK278317B6/en unknown
- 1986-10-17 CZ CS867526A patent/CZ280727B6/en not_active IP Right Cessation
- 1986-10-21 YU YU179686A patent/YU47185B/en unknown
- 1986-10-21 SI SI8611796A patent/SI8611796B/en unknown
- 1986-10-22 ZA ZA868012A patent/ZA868012B/en unknown
- 1986-10-22 CA CA000521121A patent/CA1329157C/en not_active Expired - Lifetime
- 1986-10-22 DD DD29546886A patent/DD260517A5/en not_active IP Right Cessation
- 1986-10-23 EP EP86114731A patent/EP0219874B1/en not_active Expired - Lifetime
- 1986-10-23 ES ES86114731T patent/ES2061434T3/en not_active Expired - Lifetime
- 1986-10-23 ES ES90109721T patent/ES2020498T3/en not_active Expired - Lifetime
- 1986-10-23 WO PCT/EP1986/000610 patent/WO1987002673A2/en active IP Right Grant
- 1986-10-23 AU AU65993/86A patent/AU590029B2/en not_active Ceased
- 1986-10-23 KR KR1019870700536A patent/KR900009139B1/en not_active IP Right Cessation
- 1986-10-23 HU HU865290A patent/HUT43643A/en unknown
- 1986-10-23 JP JP61505882A patent/JPH0728745B2/en not_active Expired - Lifetime
- 1986-10-23 EP EP90109721A patent/EP0393725B1/en not_active Expired - Lifetime
- 1986-10-23 AT AT86114731T patent/ATE98648T1/en not_active IP Right Cessation
- 1986-10-23 PT PT83609A patent/PT83609B/en not_active IP Right Cessation
- 1986-10-23 UA UA4202987A patent/UA6023A1/en unknown
- 1986-10-23 DE DE3650449T patent/DE3650449D1/en not_active Expired - Lifetime
- 1986-10-23 HU HU865290A patent/HU204855B/en unknown
- 1986-10-23 EP EP86906320A patent/EP0253823A1/en active Pending
- 1986-10-23 DE DE86114731T patent/DE3689404D1/en not_active Expired - Lifetime
- 1986-10-23 AT AT90109721T patent/ATE131489T1/en not_active IP Right Cessation
-
1987
- 1987-06-22 FI FI872753A patent/FI94050C/en not_active IP Right Cessation
- 1987-06-22 SU SU874202987Q patent/SU1607689A3/en active
- 1987-06-23 DK DK198703203A patent/DK175091B1/en not_active IP Right Cessation
-
1989
- 1989-09-13 AU AU41321/89A patent/AU607083B2/en not_active Expired
-
1991
- 1991-04-12 JP JP3079762A patent/JPH0824594B2/en not_active Expired - Lifetime
-
1992
- 1992-08-31 GR GR92300062T patent/GR920300062T1/en unknown
- 1992-10-16 HR HRP-1796/86A patent/HRP921075B1/en not_active IP Right Cessation
-
1993
- 1993-09-03 FI FI933868A patent/FI95578C/en not_active IP Right Cessation
-
1995
- 1995-12-14 GR GR950403376T patent/GR3018410T3/en unknown
-
1996
- 1996-08-08 HK HK153596A patent/HK153596A/en not_active IP Right Cessation
- 1996-08-08 HK HK153496A patent/HK153496A/en not_active IP Right Cessation
-
2000
- 2000-12-18 DK DK200001897A patent/DK175109B1/en not_active IP Right Cessation
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
AU609645B2 (en) * | 1988-10-17 | 1991-05-02 | Boehringer Mannheim Gmbh | Process for the activation of gene-technologically produced, biologically-active proteins expressed in prokaryotes |
WO1992004382A1 (en) * | 1990-09-05 | 1992-03-19 | Bunge (Australia) Pty. Ltd. | Solubilization of proteins in active forms |
Also Published As
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