DE69233245T2 - Verfahren zur Herstellung von Peptiden - Google Patents
Verfahren zur Herstellung von Peptiden Download PDFInfo
- Publication number
- DE69233245T2 DE69233245T2 DE69233245T DE69233245T DE69233245T2 DE 69233245 T2 DE69233245 T2 DE 69233245T2 DE 69233245 T DE69233245 T DE 69233245T DE 69233245 T DE69233245 T DE 69233245T DE 69233245 T2 DE69233245 T2 DE 69233245T2
- Authority
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- Germany
- Prior art keywords
- peptide
- fusion protein
- target
- linker
- target peptide
- 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 - Fee Related
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- 239000012149 elution buffer Substances 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 2
- 238000011835 investigation Methods 0.000 description 2
- UEGPKNKPLBYCNK-UHFFFAOYSA-L magnesium acetate Chemical compound [Mg+2].CC([O-])=O.CC([O-])=O UEGPKNKPLBYCNK-UHFFFAOYSA-L 0.000 description 2
- 239000011654 magnesium acetate Substances 0.000 description 2
- 235000011285 magnesium acetate Nutrition 0.000 description 2
- 229940069446 magnesium acetate Drugs 0.000 description 2
- 229910001629 magnesium chloride Inorganic materials 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 229960004452 methionine Drugs 0.000 description 2
- 229910000402 monopotassium phosphate Inorganic materials 0.000 description 2
- 235000019796 monopotassium phosphate Nutrition 0.000 description 2
- 230000017095 negative regulation of cell growth Effects 0.000 description 2
- PJNZPQUBCPKICU-UHFFFAOYSA-N phosphoric acid;potassium Chemical compound [K].OP(O)(O)=O PJNZPQUBCPKICU-UHFFFAOYSA-N 0.000 description 2
- 235000011056 potassium acetate Nutrition 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 239000012134 supernatant fraction Substances 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 239000012588 trypsin Substances 0.000 description 2
- NLIVDORGVGAOOJ-MAHBNPEESA-M xylene cyanol Chemical compound [Na+].C1=C(C)C(NCC)=CC=C1C(\C=1C(=CC(OS([O-])=O)=CC=1)OS([O-])=O)=C\1C=C(C)\C(=[NH+]/CC)\C=C/1 NLIVDORGVGAOOJ-MAHBNPEESA-M 0.000 description 2
- 102000003670 Carboxypeptidase B Human genes 0.000 description 1
- 108090000087 Carboxypeptidase B Proteins 0.000 description 1
- 108010035563 Chloramphenicol O-acetyltransferase Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 229910021591 Copper(I) chloride Inorganic materials 0.000 description 1
- 230000004544 DNA amplification Effects 0.000 description 1
- 238000012270 DNA recombination Methods 0.000 description 1
- 241000588722 Escherichia Species 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 101100113986 Homo sapiens CNP gene Proteins 0.000 description 1
- FFEARJCKVFRZRR-UHFFFAOYSA-N L-Methionine Natural products CSCCC(N)C(O)=O FFEARJCKVFRZRR-UHFFFAOYSA-N 0.000 description 1
- 229930195722 L-methionine Natural products 0.000 description 1
- ZJWIXBZTAAJERF-IHRRRGAJSA-N Lys-Lys-Arg Chemical compound NCCCC[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(O)=O)CCCN=C(N)N ZJWIXBZTAAJERF-IHRRRGAJSA-N 0.000 description 1
- 235000006679 Mentha X verticillata Nutrition 0.000 description 1
- 235000002899 Mentha suaveolens Nutrition 0.000 description 1
- 235000001636 Mentha x rotundifolia Nutrition 0.000 description 1
- 101800005149 Peptide B Proteins 0.000 description 1
- 101710118538 Protease Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 108010006785 Taq Polymerase Proteins 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 230000002862 amidating effect Effects 0.000 description 1
- 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
- 230000015556 catabolic process Effects 0.000 description 1
- 239000013043 chemical agent Substances 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- OXBLHERUFWYNTN-UHFFFAOYSA-M copper(I) chloride Chemical compound [Cu]Cl OXBLHERUFWYNTN-UHFFFAOYSA-M 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 229910000396 dipotassium phosphate Inorganic materials 0.000 description 1
- 235000019797 dipotassium phosphate Nutrition 0.000 description 1
- 229910000397 disodium phosphate Inorganic materials 0.000 description 1
- 235000019800 disodium phosphate Nutrition 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 238000004043 dyeing Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 238000012215 gene cloning Methods 0.000 description 1
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 239000002480 mineral oil Substances 0.000 description 1
- 235000010446 mineral oil Nutrition 0.000 description 1
- 238000005192 partition Methods 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- WROMPOXWARCANT-UHFFFAOYSA-N tfa trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F.OC(=O)C(F)(F)F WROMPOXWARCANT-UHFFFAOYSA-N 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 238000005406 washing Methods 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
- C07K14/575—Hormones
- C07K14/58—Atrial natriuretic factor complex; Atriopeptin; Atrial natriuretic peptide [ANP]; Cardionatrin; Cardiodilatin
-
- 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
- C07K14/575—Hormones
- C07K14/585—Calcitonins
-
- 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)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2468—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1) acting on beta-galactose-glycoside bonds, e.g. carrageenases (3.2.1.83; 3.2.1.157); beta-agarase (3.2.1.81)
- C12N9/2471—Beta-galactosidase (3.2.1.23), i.e. exo-(1-->4)-beta-D-galactanase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01023—Beta-galactosidase (3.2.1.23), i.e. exo-(1-->4)-beta-D-galactanase
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/50—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
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Wood Science & Technology (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biophysics (AREA)
- Biotechnology (AREA)
- Medicinal Chemistry (AREA)
- Toxicology (AREA)
- Endocrinology (AREA)
- Microbiology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Cardiology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP23076991 | 1991-08-19 | ||
| JP23076991 | 1991-08-19 | ||
| JP22352092A JP3531947B2 (ja) | 1991-08-19 | 1992-07-31 | ペプチドの製造方法 |
| JP22352092 | 1992-07-31 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| DE69233245D1 DE69233245D1 (de) | 2003-12-11 |
| DE69233245T2 true DE69233245T2 (de) | 2004-04-22 |
Family
ID=26525519
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DE69233245T Expired - Fee Related DE69233245T2 (de) | 1991-08-19 | 1992-08-19 | Verfahren zur Herstellung von Peptiden |
Country Status (6)
| Country | Link |
|---|---|
| EP (1) | EP0528686B8 (enExample) |
| AT (1) | ATE253639T1 (enExample) |
| CA (1) | CA2076320C (enExample) |
| DE (1) | DE69233245T2 (enExample) |
| ES (1) | ES2206443T3 (enExample) |
| HU (1) | HU216335B (enExample) |
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6037145A (en) * | 1994-09-07 | 2000-03-14 | Suntory Limited | Process for production of protein |
| AU700605B2 (en) * | 1994-12-07 | 1999-01-07 | Bionebraska, Inc. | Production of peptides using recombinant fusion protein constructs |
| AU4415796A (en) * | 1994-12-07 | 1996-06-26 | Bionebraska, Inc. | Production of c-terminal amidated peptides from recombinant protein constructs |
| CZ321497A3 (cs) | 1995-04-11 | 1998-06-17 | Merck And Co., Inc. | Způsob vhodný pro produkci látek, jejichž základ tvoří dipeptid |
| IL118473A0 (en) * | 1995-06-02 | 1996-09-12 | Suntory Ltd | Staphylococcus aureus V8 protease genes coding therefor and a method for the production thereof |
| DE19535445A1 (de) * | 1995-09-23 | 1997-03-27 | Boehringer Mannheim Gmbh | Verfahren zur Herstellung von natriuretischen Peptiden über Streptavidin-Fusionsproteine |
| JP2000500019A (ja) * | 1995-11-16 | 2000-01-11 | ロシュ ダイアグノスティクス ゲゼルシャフト ミット ベシュレンクテル ハフツング | ストレプトアビジン融合タンパク質経由でのペプチドの生産方法 |
| CN1242062C (zh) * | 1998-07-10 | 2006-02-15 | 赛欧斯公司 | 生产等电点高于8或低于5的多肽的方法 |
| US20020090646A1 (en) * | 2000-05-03 | 2002-07-11 | Amgen Inc. | Calcitonin-related molecules |
| IL142118A0 (en) * | 2001-03-20 | 2002-03-10 | Prochon Biotech Ltd | Method and composition for treatment of skeletal dysplasias |
| SG159387A1 (en) | 2002-11-26 | 2010-03-30 | Biocon Ltd In | Modified natriuretic compounds, conjugates, and uses thereof |
| CA2540446A1 (en) | 2003-09-30 | 2005-04-07 | Daiichi Asubio Pharma Co., Ltd. | Polypeptide cleavage method using ompt protease variant |
| JP2024520699A (ja) * | 2021-06-02 | 2024-05-24 | トパス セラピューティクス ゲーエムベーハー | Ｎ末端リンカーを含むペプチドを含むナノ粒子 |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DK175535B1 (da) * | 1987-03-04 | 2004-11-29 | Daiichi Suntory Pharma Co Ltd | Fremgangsmåde til fremstilling af et fysiologisk aktivt cysteinholdigt peptid |
-
1992
- 1992-08-12 AT AT92307577T patent/ATE253639T1/de not_active IP Right Cessation
- 1992-08-18 CA CA002076320A patent/CA2076320C/en not_active Expired - Fee Related
- 1992-08-19 DE DE69233245T patent/DE69233245T2/de not_active Expired - Fee Related
- 1992-08-19 ES ES92307577T patent/ES2206443T3/es not_active Expired - Lifetime
- 1992-08-19 EP EP92307577A patent/EP0528686B8/en not_active Expired - Lifetime
- 1992-08-19 HU HU9202688A patent/HU216335B/hu not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| DE69233245D1 (de) | 2003-12-11 |
| CA2076320C (en) | 2003-10-07 |
| EP0528686B8 (en) | 2004-01-14 |
| EP0528686A2 (en) | 1993-02-24 |
| EP0528686B1 (en) | 2003-11-05 |
| AU2107892A (en) | 1993-03-11 |
| ATE253639T1 (de) | 2003-11-15 |
| HUT62335A (en) | 1993-04-28 |
| CA2076320A1 (en) | 1993-02-20 |
| EP0528686A3 (enExample) | 1994-04-06 |
| ES2206443T3 (es) | 2004-05-16 |
| AU656791B2 (en) | 1995-02-16 |
| HU216335B (hu) | 1999-06-28 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| 8327 | Change in the person/name/address of the patent owner |
Owner name: DAIICHI ASUBIO PHARMA CO., LTD., TOKIO/TOKYO, JP |
|
| 8327 | Change in the person/name/address of the patent owner |
Owner name: ASUBIO PHARMA CO., LTD., TOKYO, JP |
|
| 8364 | No opposition during term of opposition | ||
| 8339 | Ceased/non-payment of the annual fee |