JPH11511759A - 変性タンパク質の活性化方法 - Google Patents
変性タンパク質の活性化方法Info
- Publication number
- JPH11511759A JPH11511759A JP10500957A JP50095798A JPH11511759A JP H11511759 A JPH11511759 A JP H11511759A JP 10500957 A JP10500957 A JP 10500957A JP 50095798 A JP50095798 A JP 50095798A JP H11511759 A JPH11511759 A JP H11511759A
- Authority
- JP
- Japan
- Prior art keywords
- protein
- disulfide
- mmol
- concentration
- component
- 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
-
- 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
- C07K14/475—Growth factors; Growth regulators
- C07K14/48—Nerve growth factor [NGF]
-
- 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
- C07K14/745—Blood coagulation or fibrinolysis factors
-
- 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)
-
- 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)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biomedical Technology (AREA)
- Gastroenterology & Hepatology (AREA)
- Microbiology (AREA)
- Toxicology (AREA)
- General Engineering & Computer Science (AREA)
- General Chemical & Material Sciences (AREA)
- Analytical Chemistry (AREA)
- Hematology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Abstract
Description
Claims (1)
- 【特許請求の範囲】 1.タンパク質とジスルフィド成分から構成された混合ジスルフィドの製法で あって、不活性、難溶性形態における上記タンパク質が、変性濃度における溶液 と共に、かつ、ジスルフィド成分の存在中で、インキュベートされ、それに溶解 され、そしてそれにより誘導体化される前記製法。 2.前記ジスルフィド成分が誘導体化後に除去される、請求項1に記載の製法 。 3.前記誘導体化が酸性条件下で行われる、請求項1又は2に記載の製法。 4.前記タンパク質上の遊離SH基がEDTAの添加により保護される、請求項1〜 3に記載の製法。 5.前記GSSG、シスタミン又はシステインがジスルフィド成分として使用され る、請求項1〜4に記載の製法。 6.ジスルフィド成分が少なくとも1mmol/lの濃度において使用される、請 求項1〜5に記載の製法。 7.原核生物における組換え製造後に得られることができるその不活性の難溶 性形態からの生物学的に活性なタンパク質の製法であって、その不活性な難溶性 形態におけるタンパク質が変性濃度における変性剤の溶液により、かつ、ジスル フィド成分の存在下で溶解され、その溶解されたタンパク質が、上記の強い変性 溶液を非変性又は弱い変性溶液に変更することにより生物学的に活性なコンホメ ーションを呈し、それによりそのジスルフィド成分とのジスルフィド結合が、破 壊され、そしてそのタンパク質がそれを生物学的に活性ならしめるコンホメーシ ョンを採用することができるような方法で、そのタンパク質内に分子内で新たに 形成される、前記製法。 8.前記の再生されたタンパク質がプロテアーゼ、成長因子、タンパク質ホル モン、ニュートロフィン又はサイトカインである、請求項7に記載の製法。
Applications Claiming Priority (5)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP96109288.9 | 1996-06-11 | ||
EP96109288 | 1996-06-11 | ||
EP96110109.4 | 1996-06-22 | ||
EP96110109 | 1996-06-22 | ||
PCT/EP1997/003026 WO1997047735A1 (de) | 1996-06-11 | 1997-06-11 | Verfahren zur aktivierung von denaturiertem protein |
Publications (2)
Publication Number | Publication Date |
---|---|
JPH11511759A true JPH11511759A (ja) | 1999-10-12 |
JP3288720B2 JP3288720B2 (ja) | 2002-06-04 |
Family
ID=26141986
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP50095798A Expired - Lifetime JP3288720B2 (ja) | 1996-06-11 | 1997-06-11 | 変性タンパク質の活性化方法 |
Country Status (12)
Country | Link |
---|---|
US (1) | US6342585B1 (ja) |
EP (1) | EP0904355B1 (ja) |
JP (1) | JP3288720B2 (ja) |
KR (1) | KR100305341B1 (ja) |
AT (1) | ATE260972T1 (ja) |
AU (1) | AU714318B2 (ja) |
BR (1) | BR9709569B1 (ja) |
CA (1) | CA2257122C (ja) |
DE (1) | DE59711375D1 (ja) |
ES (1) | ES2214624T3 (ja) |
TR (1) | TR199802584T2 (ja) |
WO (1) | WO1997047735A1 (ja) |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2004525601A (ja) * | 1999-12-01 | 2004-08-26 | メルク パテント ゲゼルシャフト ミット ベシュレンクテル ハフトング | IgE反応性の低減した昆虫毒アレルゲンおよびその製造方法 |
Families Citing this family (15)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DE59810555D1 (de) | 1998-10-09 | 2004-02-12 | Scil Proteins Gmbh | Verfahren zur Gewinnung von aktivem Beta-NGF |
US20040223967A1 (en) * | 2000-05-24 | 2004-11-11 | Riken | Blood coagulation factor-activating protein and antibody thereto |
AU2001273348A1 (en) * | 2000-07-10 | 2002-01-21 | Diosynth Rtp, Inc. | Purification of human troponin i |
US7112570B2 (en) * | 2000-08-24 | 2006-09-26 | Neuren Pharmaceuticals, Ltd. | GPE analogs |
DE10105912A1 (de) * | 2001-02-09 | 2002-08-14 | Roche Diagnostics Gmbh | Rekombinante Proteinase K |
US7605177B2 (en) | 2001-05-24 | 2009-10-20 | Neuren Pharmaceuticals Limited | Effects of glycyl-2 methyl prolyl glutamate on neurodegeneration |
US20070004641A1 (en) * | 2001-05-24 | 2007-01-04 | Neuren Pharmaceuticals Limited | Cognitive enhancement and cognitive therapy using glycyl-L-2-methylprolyl-L-glutamate |
US7714020B2 (en) | 2001-05-24 | 2010-05-11 | Neuren Pharmaceuticals Limited | Treatment of non-convulsive seizures in brain injury using G-2-methyl-prolyl glutamate |
ES2325983T3 (es) | 2001-05-24 | 2009-09-28 | Neuren Pharmaceuticals Limited | Analogos y peptidomimeticos de gpe. |
AU2002354363A1 (en) * | 2001-12-04 | 2003-06-17 | Mitsubishi Pharma Corporation | Method of activating protein |
DE10224111A1 (de) * | 2002-05-29 | 2003-12-18 | November Ag Molekulare Medizin | Verfahren zum Assemblieren von Untereinheiten zu Kapsoiden |
AU2003259846A1 (en) * | 2002-08-16 | 2004-03-03 | The General Hospital Corporation | Non-invasive functional imaging of peripheral nervous system activation in humans and animals |
US20060257393A1 (en) * | 2002-12-20 | 2006-11-16 | Kenji Sasaki | Method for protecting thiol group of protein |
US20080131500A1 (en) * | 2006-12-04 | 2008-06-05 | The Board Of Regents Of The University Of Texas System | Methods and compositions for rapid inactivation of proteins |
CA2862820A1 (en) * | 2012-02-29 | 2013-09-06 | F. Hoffmann-La Roche Ag | On-column enzymatic cleavage |
Family Cites Families (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
AU141204B (en) | 1904-08-30 | 1905-07-18 | William Trewiiella | Improved pawl and ratchet mechanism |
GR79124B (ja) * | 1982-12-22 | 1984-10-02 | Genentech Inc | |
US4923767A (en) * | 1985-06-18 | 1990-05-08 | International Fuel Cells | Fuel cell power plants employing an aqueous solution |
DE3537708A1 (de) * | 1985-10-23 | 1987-04-23 | Boehringer Mannheim Gmbh | Verfahren zur aktivierung von t-pa nach expression in prokaryonten |
US4766205A (en) * | 1985-11-13 | 1988-08-23 | Beatrice Companies, Inc. | Method for isolation of recombinant polypeptides in biologically active forms |
EP0301835A1 (en) | 1987-07-29 | 1989-02-01 | Schering Biotech Corporation | Purification of human interleukin-4 expressed in Escherichia Coli |
DE3832898A1 (de) * | 1988-09-28 | 1990-04-12 | Boehringer Mannheim Gmbh | Praeparat von in prokaryonten exprimiertem plasminogenaktivator |
US5235043A (en) * | 1990-04-06 | 1993-08-10 | Synergen, Inc. | Production of biologically active, recombinant members of the ngf/bdnf family of neurotrophic proteins |
-
1997
- 1997-06-11 AU AU32571/97A patent/AU714318B2/en not_active Expired
- 1997-06-11 CA CA002257122A patent/CA2257122C/en not_active Expired - Lifetime
- 1997-06-11 AT AT97928173T patent/ATE260972T1/de active
- 1997-06-11 DE DE59711375T patent/DE59711375D1/de not_active Expired - Lifetime
- 1997-06-11 EP EP97928173A patent/EP0904355B1/de not_active Expired - Lifetime
- 1997-06-11 JP JP50095798A patent/JP3288720B2/ja not_active Expired - Lifetime
- 1997-06-11 BR BRPI9709569-9A patent/BR9709569B1/pt not_active IP Right Cessation
- 1997-06-11 KR KR1019980710184A patent/KR100305341B1/ko not_active IP Right Cessation
- 1997-06-11 WO PCT/EP1997/003026 patent/WO1997047735A1/de active IP Right Grant
- 1997-06-11 ES ES97928173T patent/ES2214624T3/es not_active Expired - Lifetime
- 1997-06-11 TR TR1998/02584T patent/TR199802584T2/xx unknown
- 1997-06-11 US US09/202,206 patent/US6342585B1/en not_active Expired - Lifetime
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2004525601A (ja) * | 1999-12-01 | 2004-08-26 | メルク パテント ゲゼルシャフト ミット ベシュレンクテル ハフトング | IgE反応性の低減した昆虫毒アレルゲンおよびその製造方法 |
Also Published As
Publication number | Publication date |
---|---|
KR100305341B1 (ko) | 2002-03-02 |
KR20000016588A (ko) | 2000-03-25 |
AU714318B2 (en) | 2000-01-06 |
CA2257122C (en) | 2004-04-06 |
JP3288720B2 (ja) | 2002-06-04 |
AU3257197A (en) | 1998-01-07 |
US6342585B1 (en) | 2002-01-29 |
WO1997047735A1 (de) | 1997-12-18 |
EP0904355B1 (de) | 2004-03-03 |
EP0904355A1 (de) | 1999-03-31 |
CA2257122A1 (en) | 1997-12-18 |
BR9709569A (pt) | 1999-08-10 |
BR9709569B1 (pt) | 2010-05-18 |
DE59711375D1 (de) | 2004-04-08 |
TR199802584T2 (xx) | 1999-03-22 |
ES2214624T3 (es) | 2004-09-16 |
ATE260972T1 (de) | 2004-03-15 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JP3288720B2 (ja) | 変性タンパク質の活性化方法 | |
US8501439B2 (en) | Method for obtaining active pro-NGF and beta-NGF | |
DK175109B1 (da) | Fremgangsmåde til aktivering af genteknologisk fremstillede, heterologe, disulfidbroer indeholdende eukaryotiske proteiner efter ekspression i prokaryotiske celler | |
Marston et al. | [20] Solubilization of protein aggregates | |
Patra et al. | Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli | |
JP2592981B2 (ja) | タンパク質アミノ末端配列の酸素的除去 | |
JPH02142490A (ja) | 組換えタンパク質の精製と再生 | |
JP2004516300A (ja) | 化学的に合成したポリペプチドをフォールディングする方法 | |
Opitz et al. | Proteolytic dimers of porcine muscle lactate dehydrogenase: characterization, folding, and reconstitution of the truncated and nicked polypeptide chain | |
BRPI9914393B1 (pt) | Método para a preparação de pro-ngf biologicamente ativo, bem como uso de pro-ngf recombinante | |
Estape et al. | Susceptibility towards intramolecular disulphide-bond formation affects conformational stability and folding of human basic fibroblast growth factor | |
JP2001008697A (ja) | E.コリでの非融合タンパク質の調製方法 | |
KR100554490B1 (ko) | 분자내 샤퍼론 유사 서열을 함유하는 키메라 단백질 및이것의 인슐린 제조용 용도 | |
Wallner et al. | Lab scale and medium scale production of recombinant allergens in Escherichia coli | |
WO1990004035A1 (en) | Recombinant pdgf and methods for production | |
Hoefkens et al. | Isolation, renaturation and partial characterization of recombinant human transferrin and its half molecules from Escherichia coli | |
JP3070935B2 (ja) | 変性組換え融合蛋白質のバイオ触媒的な正確な鎖フオールデイングのための方法 | |
Holtet et al. | Receptor‐binding domain of human α2‐macroglobulin Expression, folding and biochemical characterization of a high‐affinity recombinant derivative | |
Denigris et al. | Expression of bovine seminal ribonuclease in Escherichia coli | |
IE62228B1 (en) | A method for the selective cleavage of fusion proteins | |
JP3932475B2 (ja) | 新規フェリチン | |
JP3004788B2 (ja) | アルギニンデイミナーゼ発現ベクター、形質転換微生物およびアルギニンデイミナーゼの製造法 | |
RU2143492C1 (ru) | Рекомбинантная плазмида, кодирующая гибридный белок - предшественник инсулина человека (варианты), штамм бактерий e.coli - продуцент гибридного белка - предшественника инсулина человека (варианты), способ получения инсулина человека | |
JPH0923883A (ja) | 遺伝子操作による生物活性β−NGFの生産方法 | |
EP0578472A2 (en) | A process for recovering peptides expressed as fusion proteins |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20090315 Year of fee payment: 7 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20100315 Year of fee payment: 8 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20100315 Year of fee payment: 8 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20110315 Year of fee payment: 9 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20110315 Year of fee payment: 9 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20130315 Year of fee payment: 11 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20140315 Year of fee payment: 12 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
EXPY | Cancellation because of completion of term |