JP4820512B2 - タンパク質の製造 - Google Patents
タンパク質の製造 Download PDFInfo
- Publication number
- JP4820512B2 JP4820512B2 JP2001515842A JP2001515842A JP4820512B2 JP 4820512 B2 JP4820512 B2 JP 4820512B2 JP 2001515842 A JP2001515842 A JP 2001515842A JP 2001515842 A JP2001515842 A JP 2001515842A JP 4820512 B2 JP4820512 B2 JP 4820512B2
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- Prior art keywords
- pro
- polypeptide
- cleavage
- fusion protein
- terminus
- 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.)
- Expired - Lifetime
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- 235000003704 aspartic acid Nutrition 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 101150049515 bla gene Proteins 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 230000000120 cytopathologic effect Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 239000003398 denaturant Substances 0.000 description 1
- 238000010217 densitometric analysis Methods 0.000 description 1
- 239000006185 dispersion Substances 0.000 description 1
- 238000011143 downstream manufacturing Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 229940105423 erythropoietin Drugs 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 210000003754 fetus Anatomy 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 101150045500 galK gene Proteins 0.000 description 1
- 101150041954 galU gene Proteins 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 101150096208 gtaB gene Proteins 0.000 description 1
- 230000003394 haemopoietic effect Effects 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 239000003262 industrial enzyme Substances 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 229940047122 interleukins Drugs 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- JEIPFZHSYJVQDO-UHFFFAOYSA-N iron(III) oxide Inorganic materials O=[Fe]O[Fe]=O JEIPFZHSYJVQDO-UHFFFAOYSA-N 0.000 description 1
- YOBAEOGBNPPUQV-UHFFFAOYSA-N iron;trihydrate Chemical compound O.O.O.[Fe].[Fe] YOBAEOGBNPPUQV-UHFFFAOYSA-N 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 235000018977 lysine Nutrition 0.000 description 1
- 230000002934 lysing effect Effects 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L magnesium chloride Substances [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 101150079876 mcrB gene Proteins 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000002906 microbiologic effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 102000034288 naturally occurring fusion proteins Human genes 0.000 description 1
- 108091006048 naturally occurring fusion proteins Proteins 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 101150012154 nupG gene Proteins 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 230000001817 pituitary effect Effects 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000012805 post-processing Methods 0.000 description 1
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 230000007026 protein scission Effects 0.000 description 1
- 230000012743 protein tagging Effects 0.000 description 1
- 230000007420 reactivation Effects 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000007363 ring formation reaction Methods 0.000 description 1
- 230000028043 self proteolysis Effects 0.000 description 1
- 239000011537 solubilization buffer Substances 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 239000011550 stock solution Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 238000011282 treatment Methods 0.000 description 1
- 238000011269 treatment regimen Methods 0.000 description 1
- 229960005486 vaccine Drugs 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000010626 work up procedure Methods 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
Classifications
-
- 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
- C07K14/54—Interleukins [IL]
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
-
- 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)
- C12N9/503—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from viruses
- C12N9/506—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from viruses derived from RNA viruses
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/20—Fusion polypeptide containing a tag with affinity for a non-protein ligand
- C07K2319/21—Fusion polypeptide containing a tag with affinity for a non-protein ligand containing a His-tag
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/50—Fusion polypeptide containing protease site
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
- C07K2319/75—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor containing a fusion for activation of a cell surface receptor, e.g. thrombopoeitin, NPY and other peptide hormones
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Molecular Biology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Microbiology (AREA)
- Virology (AREA)
- Biophysics (AREA)
- Medicinal Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Enzymes And Modification Thereof (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AT1367/99 | 1999-08-09 | ||
| AT136799 | 1999-08-09 | ||
| PCT/EP2000/007643 WO2001011057A1 (en) | 1999-08-09 | 2000-08-07 | Production of proteins |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2003506093A JP2003506093A (ja) | 2003-02-18 |
| JP2003506093A5 JP2003506093A5 (https=) | 2007-09-27 |
| JP4820512B2 true JP4820512B2 (ja) | 2011-11-24 |
Family
ID=3512357
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2001515842A Expired - Lifetime JP4820512B2 (ja) | 1999-08-09 | 2000-08-07 | タンパク質の製造 |
Country Status (21)
| Country | Link |
|---|---|
| US (2) | US6936455B1 (https=) |
| EP (1) | EP1200604B1 (https=) |
| JP (1) | JP4820512B2 (https=) |
| KR (1) | KR20020026366A (https=) |
| CN (1) | CN1230543C (https=) |
| AT (1) | ATE335826T1 (https=) |
| AU (1) | AU775662B2 (https=) |
| CA (1) | CA2379571C (https=) |
| CZ (1) | CZ302366B6 (https=) |
| DE (1) | DE60029968T2 (https=) |
| ES (1) | ES2269173T3 (https=) |
| HK (1) | HK1047128B (https=) |
| HU (1) | HU230231B1 (https=) |
| IL (1) | IL147456A0 (https=) |
| MX (1) | MXPA02001424A (https=) |
| NO (1) | NO328339B1 (https=) |
| NZ (1) | NZ516869A (https=) |
| PL (1) | PL200225B1 (https=) |
| SK (1) | SK287488B6 (https=) |
| TR (1) | TR200200253T2 (https=) |
| WO (1) | WO2001011057A1 (https=) |
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| TR200200048T2 (tr) * | 1999-08-09 | 2002-04-22 | Biochemie Gesellschaft M.B.H. | Otoproteolitik klevaj vasıtasıyla proteinlerin üretimi. |
| ES2453048T3 (es) | 2004-03-30 | 2014-04-03 | Relypsa, Inc. | Polímeros de unión de ión y usos de los mismos |
| PL1874825T3 (pl) * | 2005-04-26 | 2011-04-29 | Boehringer Ingelheim Rcv Gmbh | Ligandy powinowactwa |
| AU2011253661B2 (en) * | 2005-04-26 | 2013-06-13 | Boehringer Ingelheim Rcv Gmbh & Co Kg | Production of recombinant proteins by autoproteolytic cleavage of a fusion protein |
| GB0508434D0 (en) * | 2005-04-26 | 2005-06-01 | Sandoz Ag | Organic compounds |
| GB0508435D0 (en) * | 2005-04-26 | 2005-06-01 | Sandoz Ag | Organic compounds |
| CN103069000A (zh) | 2010-08-31 | 2013-04-24 | 天野酶株式会社 | 使用了酶的蛋壳膜的溶解方法 |
| EP2684951A1 (en) | 2012-07-13 | 2014-01-15 | Sandoz Ag | Method for producing a recombinant protein of interest |
| EP2746390A1 (en) * | 2012-12-19 | 2014-06-25 | Sandoz Ag | Method for producing a recombinant protein of interest |
| EP2746391A1 (en) | 2012-12-19 | 2014-06-25 | Sandoz Ag | Method for producing a recombinant protein of interest |
| UY35874A (es) | 2013-12-12 | 2015-07-31 | Novartis Ag | Un proceso para la preparación de una composición de proteínas pegiladas |
| RU2619217C1 (ru) * | 2015-12-04 | 2017-05-12 | Федеральное государственное бюджетное учреждение "Государственный научно-исследовательский институт генетики и селекции промышленных микроорганизмов" (ФГБУ "ГосНИИгенетика") | Температурочувствительный мутантный интеин для нерастворимой экспрессии предшественника целевого белка |
| CN114539425B (zh) * | 2022-02-25 | 2023-04-28 | 湖南中晟全肽生化有限公司 | 一种提高线性多肽生物表达的方法 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1998049326A1 (en) * | 1997-04-25 | 1998-11-05 | Sembiosys Genetics Inc. | Method for cleavage of fusion proteins |
| WO1999010503A1 (de) * | 1997-08-22 | 1999-03-04 | Roche Diagnostics Gmbh | Autokatalytisch aktivierbare zymogene vorstufen von proteasen und deren verwendung |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4743679A (en) | 1986-02-24 | 1988-05-10 | Creative Biomolecules, Inc. | Process for producing human epidermal growth factor and analogs thereof |
| EP0321973B1 (de) * | 1987-12-23 | 1993-11-03 | BOEHRINGER INGELHEIM INTERNATIONAL GmbH | Expression der viral kodierten Protease P2A des HRV2 |
| WO1999010483A2 (de) | 1997-08-22 | 1999-03-04 | Roche Diagnostics Gmbh | Autokatalytisch aktivierbare vorstufen von proteasen und deren verwendung |
-
2000
- 2000-08-07 PL PL353101A patent/PL200225B1/pl unknown
- 2000-08-07 CA CA2379571A patent/CA2379571C/en not_active Expired - Lifetime
- 2000-08-07 JP JP2001515842A patent/JP4820512B2/ja not_active Expired - Lifetime
- 2000-08-07 MX MXPA02001424A patent/MXPA02001424A/es unknown
- 2000-08-07 NZ NZ516869A patent/NZ516869A/en not_active IP Right Cessation
- 2000-08-07 AT AT00958389T patent/ATE335826T1/de active
- 2000-08-07 HK HK02107014.5A patent/HK1047128B/en not_active IP Right Cessation
- 2000-08-07 HU HU0202519A patent/HU230231B1/hu unknown
- 2000-08-07 CZ CZ20020481A patent/CZ302366B6/cs not_active IP Right Cessation
- 2000-08-07 KR KR1020027001666A patent/KR20020026366A/ko not_active Ceased
- 2000-08-07 SK SK185-2002A patent/SK287488B6/sk not_active IP Right Cessation
- 2000-08-07 CN CNB008114595A patent/CN1230543C/zh not_active Expired - Lifetime
- 2000-08-07 WO PCT/EP2000/007643 patent/WO2001011057A1/en not_active Ceased
- 2000-08-07 TR TR2002/00253T patent/TR200200253T2/xx unknown
- 2000-08-07 US US10/048,882 patent/US6936455B1/en not_active Expired - Lifetime
- 2000-08-07 EP EP00958389A patent/EP1200604B1/en not_active Expired - Lifetime
- 2000-08-07 AU AU69933/00A patent/AU775662B2/en not_active Expired
- 2000-08-07 ES ES00958389T patent/ES2269173T3/es not_active Expired - Lifetime
- 2000-08-07 IL IL14745600A patent/IL147456A0/xx unknown
- 2000-08-07 DE DE60029968T patent/DE60029968T2/de not_active Expired - Lifetime
-
2002
- 2002-02-08 NO NO20020633A patent/NO328339B1/no not_active IP Right Cessation
-
2005
- 2005-04-05 US US11/099,302 patent/US20050186564A1/en not_active Abandoned
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1998049326A1 (en) * | 1997-04-25 | 1998-11-05 | Sembiosys Genetics Inc. | Method for cleavage of fusion proteins |
| WO1999010503A1 (de) * | 1997-08-22 | 1999-03-04 | Roche Diagnostics Gmbh | Autokatalytisch aktivierbare zymogene vorstufen von proteasen und deren verwendung |
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| EP0422049A4 (en) | Vector for secretion of proteins directly into periplasm or culture medium | |
| JPS63185385A (ja) | プラスミドベクタ− |
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