AU6599386A – Process for the activation of genetically engineered, heterologous disulfide bridge-containing eukaryotic proteins after expression in
– Google Patents
AU6599386A – Process for the activation of genetically engineered, heterologous disulfide bridge-containing eukaryotic proteins after expression in
– Google Patents
Process for the activation of genetically engineered, heterologous disulfide bridge-containing eukaryotic proteins after expression in
Info
Publication number
AU6599386A
AU6599386A
AU65993/86A
AU6599386A
AU6599386A
AU 6599386 A
AU6599386 A
AU 6599386A
AU 65993/86 A
AU65993/86 A
AU 65993/86A
AU 6599386 A
AU6599386 A
AU 6599386A
AU 6599386 A
AU6599386 A
AU 6599386A
Authority
AU
Australia
Prior art keywords
pref
expression
esp
activation
denaturing
Prior art date
1985-10-23
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
Application number
AU65993/86A
Other versions
AU590029B2
(en
Inventor
Stephan Fischer
Ralf Mattes
Rainer Rudolph
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Roche Diagnostics GmbH
Original Assignee
Boehringer Mannheim GmbH
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
1985-10-23
Filing date
1986-10-23
Publication date
1987-05-19
1986-10-23
Application filed by Boehringer Mannheim GmbH
filed
Critical
Boehringer Mannheim GmbH
1987-05-19
Publication of AU6599386A
publication
Critical
patent/AU6599386A/en
1989-10-26
Application granted
granted
Critical
1989-10-26
Publication of AU590029B2
publication
Critical
patent/AU590029B2/en
2006-10-23
Anticipated expiration
legal-status
Critical
Status
Ceased
legal-status
Critical
Current
Links
Espacenet
Global Dossier
Discuss
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)
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.
AU65993/86A
1985-10-23
1986-10-23
Process for the activation of genetically engineered, heterologous disulfide bridge-containing eukaryotic proteins after expression in
Ceased
AU590029B2
(en)
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 Child Applications (1)
Application Number
Title
Priority Date
Filing Date
AU41321/89A
Division
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
Publications (2)
Publication Number
Publication Date
AU6599386A
true
AU6599386A
(en)
1987-05-19
AU590029B2
AU590029B2
(en)
1989-10-26
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 After (1)
Application Number
Title
Priority Date
Filing Date
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
Country Status (26)
Country
Link
EP
(3)
EP0253823A1
(en)
JP
(2)
JPH0728745B2
(en)
KR
(1)
KR900009139B1
(en)
AT
(2)
ATE131489T1
(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)
HU204855B
(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 (3)
* Cited by examiner, † Cited by third party
Publication number
Priority date
Publication date
Assignee
Title
AU602664B2
(en)
*
1985-11-27
1990-10-25
Mitsui Toatsu Chemicals Inc.
DNA sequence containing the DNA sequence coding for human tissue plasminogen activator originating from human normal cells, recombinant DNA incorporating the DNA sequence, host cells transformed with the recombinant DNA, and process for producing human tissue plasminogen activator by use of the host cells
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
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US4766205A
(en)
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1985-11-13
1988-08-23
Beatrice Companies, Inc.
Method for isolation of recombinant polypeptides in biologically active forms
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
DE69126434D1
(en)
*
1990-08-20
1997-07-10
Novo Nordisk As
Process for the production of biologically active IGF-1 by using amino-terminally extended IGF-1
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
EP0586667A1
(en)
*
1992-03-24
1994-03-16
Synergen, Inc.
Refolding and purification of insulin-like growth factor i
DE59305396D1
(en)
1992-12-02
1997-03-20
Hoechst Ag
Process for obtaining proinsulin with correctly 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
US6342585B1
(en)
*
1996-06-11
2002-01-29
Roche Diagnostics 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
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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
CN1318443C
(en)
2000-05-16
2007-05-30
博尔德生物技术公司
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
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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
AR062069A1
(en)
2006-07-14
2008-10-15
Genentech Inc
REPLEGED OF RECOMBINANT PROTEINS
US8617531B2
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2006-12-14
2013-12-31
Bolder Biotechnology, Inc.
Methods of making proteins and peptides containing a single free cysteine
EA022821B1
(en)
2010-03-17
2016-03-31
Ратиофарм Гмбх
Method for obtaining biologically active recombinant human g-csf
JP2013540157A
(en)
*
2010-10-20
2013-10-31
メディミューン，エルエルシー
Method for treating inclusion bodies
HU1200171A1
(en)
2012-03-19
2013-09-30
Richter Gedeon Nyrt
Methods for the production of polypeptides
HU1200172A2
(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
CA3044371A1
(en)
2016-12-30
2018-07-05
Biogend Therapeutics Co., Ltd.
Recombinant polypeptides and nucleic acid molecules, compositions, and methods of making and uses thereof
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(en)
2020-12-18
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Richter Gedeon Nyrt.
Methods for the purification of refolded fc-peptide fusion protein
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*
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1985-07-23
Cetus Corporation
Controlled oxidation of microbially produced cysteine-containing proteins
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(en)
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1988-05-31
Cetus Corporation
Process for recovering refractile bodies containing heterologous proteins from microbial hosts
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*
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1988-08-23
Beatrice Companies, Inc.
Method for isolation of recombinant polypeptides in biologically active forms
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(en)
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CONTAINER ON PALLET WITH FOLDED AND REINFORCED MESH PROTECTION DEVICE
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(en)
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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
CZ
CS867526A
patent/CZ280727B6/en
not_active
IP Right Cessation
1986-10-17
SK
SK7526-86A
patent/SK278317B6/en
unknown
1986-10-21
SI
SI8611796A
patent/SI8611796B/en
unknown
1986-10-21
YU
YU179686A
patent/YU47185B/en
unknown
1986-10-22
DD
DD29546886A
patent/DD260517A5/en
not_active
IP Right Cessation
1986-10-22
CA
CA000521121A
patent/CA1329157C/en
not_active
Expired – Lifetime
1986-10-22
ZA
ZA868012A
patent/ZA868012B/en
unknown
1986-10-23
AT
AT90109721T
patent/ATE131489T1/en
not_active
IP Right Cessation
1986-10-23
AT
AT86114731T
patent/ATE98648T1/en
not_active
IP Right Cessation
1986-10-23
DE
DE3650449T
patent/DE3650449D1/en
not_active
Expired – Lifetime
1986-10-23
EP
EP86906320A
patent/EP0253823A1/en
active
Pending
1986-10-23
ES
ES86114731T
patent/ES2061434T3/en
not_active
Expired – Lifetime
1986-10-23
EP
EP86114731A
patent/EP0219874B1/en
not_active
Expired – Lifetime
1986-10-23
ES
ES90109721T
patent/ES2020498T3/en
not_active
Expired – Lifetime
1986-10-23
PT
PT83609A
patent/PT83609B/en
not_active
IP Right Cessation
1986-10-23
WO
PCT/EP1986/000610
patent/WO1987002673A2/en
active
IP Right Grant
1986-10-23
JP
JP61505882A
patent/JPH0728745B2/en
not_active
Expired – Lifetime
1986-10-23
KR
KR1019870700536A
patent/KR900009139B1/en
not_active
IP Right Cessation
1986-10-23
UA
UA4202987A
patent/UA6023A1/en
unknown
1986-10-23
EP
EP90109721A
patent/EP0393725B1/en
not_active
Expired – Lifetime
1986-10-23
AU
AU65993/86A
patent/AU590029B2/en
not_active
Ceased
1986-10-23
HU
HU865290A
patent/HU204855B/en
unknown
1986-10-23
DE
DE86114731T
patent/DE3689404D1/en
not_active
Expired – Lifetime
1986-10-23
HU
HU865290A
patent/HUT43643A/en
unknown
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 (3)
* Cited by examiner, † Cited by third party
Publication number
Priority date
Publication date
Assignee
Title
AU602664B2
(en)
*
1985-11-27
1990-10-25
Mitsui Toatsu Chemicals Inc.
DNA sequence containing the DNA sequence coding for human tissue plasminogen activator originating from human normal cells, recombinant DNA incorporating the DNA sequence, host cells transformed with the recombinant DNA, and process for producing human tissue plasminogen activator by use of the host cells
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
Publication number
Publication date
IL80325A0
(en)
1987-01-30
WO1987002673A2
(en)
1987-05-07
EP0393725B1
(en)
1995-12-13
CZ280727B6
(en)
1996-04-17
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