JP2000500019A - 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 - Google Patents
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Info
- Publication number
- JP2000500019A JP2000500019A JP9518551A JP51855197A JP2000500019A JP 2000500019 A JP2000500019 A JP 2000500019A JP 9518551 A JP9518551 A JP 9518551A JP 51855197 A JP51855197 A JP 51855197A JP 2000500019 A JP2000500019 A JP 2000500019A
- Authority
- JP
- Japan
- Prior art keywords
- fusion protein
- peptide
- protein
- pth
- streptavidin
- 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.)
- Ceased
Links
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- 230000029142 excretion Effects 0.000 description 1
- 238000010195 expression analysis Methods 0.000 description 1
- 229940012952 fibrinogen Drugs 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 229960000789 guanidine hydrochloride Drugs 0.000 description 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 102000058004 human PTH Human genes 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000009878 intermolecular interaction Effects 0.000 description 1
- 210000000936 intestine Anatomy 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 101150109249 lacI gene Proteins 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 210000002464 muscle smooth vascular Anatomy 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 108010073230 parathyroid hormone (1-38) Proteins 0.000 description 1
- 230000007030 peptide scission Effects 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 238000004987 plasma desorption mass spectroscopy Methods 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000012495 positive regulation of renal sodium excretion Effects 0.000 description 1
- 239000008057 potassium phosphate buffer Substances 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 108010077112 prolyl-proline Proteins 0.000 description 1
- 235000004252 protein component Nutrition 0.000 description 1
- 239000003531 protein hydrolysate Substances 0.000 description 1
- 238000000164 protein isolation Methods 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 230000006340 racemization Effects 0.000 description 1
- QGFSVPWZEPKNDV-BRTFOEFASA-N ranp Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)=O)[C@@H](C)CC)[C@@H](C)CC)C1=CC=CC=C1 QGFSVPWZEPKNDV-BRTFOEFASA-N 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 238000004611 spectroscopical analysis Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 229960001322 trypsin Drugs 0.000 description 1
- 150000003672 ureas Chemical class 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 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
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/36—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Actinomyces; from Streptomyces (G)
-
- 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
- C07K14/635—Parathyroid hormone, i.e. parathormone; Parathyroid hormone-related peptides
-
- 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
- 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
- C07K2319/22—Fusion polypeptide containing a tag with affinity for a non-protein ligand containing a Strep-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
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Molecular Biology (AREA)
- Zoology (AREA)
- Biophysics (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Endocrinology (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Toxicology (AREA)
- Physics & Mathematics (AREA)
- Microbiology (AREA)
- Plant Pathology (AREA)
- Cardiology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE19542702 | 1995-11-16 | ||
| DE19542702.5 | 1995-11-16 | ||
| PCT/EP1996/004850 WO1997018314A1 (de) | 1995-11-16 | 1996-11-06 | Verfahren zur herstellung von peptiden über streptavidin-fusionsproteine |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2000500019A true JP2000500019A (ja) | 2000-01-11 |
| JP2000500019A5 JP2000500019A5 (enExample) | 2004-11-04 |
Family
ID=7777604
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP9518551A Ceased JP2000500019A (ja) | 1995-11-16 | 1996-11-06 | 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 |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US6136564A (enExample) |
| EP (1) | EP0861325A1 (enExample) |
| JP (1) | JP2000500019A (enExample) |
| AU (1) | AU7566396A (enExample) |
| CA (1) | CA2237296C (enExample) |
| WO (1) | WO1997018314A1 (enExample) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2005517658A (ja) * | 2001-12-18 | 2005-06-16 | エイドゲントシッシュ テクニーシェ ホッシュール チューリッヒ | 組織操作のための成長因子改変タンパク質マトリクス |
Families Citing this family (35)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20020168718A1 (en) * | 1997-04-03 | 2002-11-14 | California Institute Of Technology | Enzyme-mediated modification of fibrin for tissue engineering |
| US7601685B2 (en) * | 1998-08-27 | 2009-10-13 | Eidgenossische Technische Hochschule Zurich | Growth factor modified protein matrices for tissue engineering |
| ES2368988T3 (es) | 1999-02-01 | 2011-11-24 | Eidgenössische Technische Hochschule Zürich | Bio-materiales formados por reacción de adición nucleófila a grupos insaturados conjugados. |
| US6958212B1 (en) * | 1999-02-01 | 2005-10-25 | Eidgenossische Technische Hochschule Zurich | Conjugate addition reactions for the controlled delivery of pharmaceutically active compounds |
| EP1190061A1 (en) * | 1999-06-07 | 2002-03-27 | Neorx Corporation | Streptavidin expressed gene fusions and methods of use thereof |
| US7144991B2 (en) | 1999-06-07 | 2006-12-05 | Aletheon Pharmaceuticals, Inc. | Streptavidin expressed gene fusions and methods of use thereof |
| US7291673B2 (en) * | 2000-06-02 | 2007-11-06 | Eidgenossiche Technische Hochschule Zurich | Conjugate addition reactions for the controlled delivery of pharmaceutically active compounds |
| US7247609B2 (en) | 2001-12-18 | 2007-07-24 | Universitat Zurich | Growth factor modified protein matrices for tissue engineering |
| EP1465989B1 (en) * | 2001-12-18 | 2008-02-20 | Eidgenossisch Technische Hochschule Zurich | Growth factor modified protein matrices for tissue engineering |
| US8282912B2 (en) * | 2002-03-22 | 2012-10-09 | Kuros Biosurgery, AG | Compositions for tissue augmentation |
| US8399400B2 (en) | 2004-12-01 | 2013-03-19 | Syntaxin, Ltd. | Fusion proteins |
| US8512984B2 (en) | 2004-12-01 | 2013-08-20 | Syntaxin, Ltd. | Non-cytotoxic protein conjugates |
| US8778634B2 (en) | 2004-12-01 | 2014-07-15 | Syntaxin, Ltd. | Non-cytotoxic protein conjugates |
| GB0426394D0 (en) * | 2004-12-01 | 2005-01-05 | Health Prot Agency | Fusion proteins |
| US8603779B2 (en) | 2004-12-01 | 2013-12-10 | Syntaxin, Ltd. | Non-cytotoxic protein conjugates |
| EP1828244A2 (en) * | 2004-12-22 | 2007-09-05 | Kuros Biosurgery AG | Michael-type addition reaction functionalised peg hydrogels with factor xiiia incorporated biofactors |
| ES2593051T3 (es) * | 2005-01-06 | 2016-12-05 | Kuros Biosurgery Ag | Matrices suplementadas para la reparación de fracturas óseas |
| WO2006073711A2 (en) * | 2005-01-06 | 2006-07-13 | Kuros Biosurgery Ag | Use of a matrix comprising a contrast agent in soft tissues |
| US8575101B2 (en) | 2005-01-06 | 2013-11-05 | Kuros Biosurgery Ag | Supplemented matrices for the repair of bone fractures |
| GB0610867D0 (en) | 2006-06-01 | 2006-07-12 | Syntaxin Ltd | Treatment of pain |
| PT2136850E (pt) * | 2007-04-13 | 2012-04-27 | Kuros Biosurgery Ag | Selante tecidual polimérico |
| CA2710798A1 (en) * | 2007-12-28 | 2009-07-09 | Kuros Biosurgery Ag | Pdgf fusion proteins incorporated into fibrin foams |
| AU2010230563A1 (en) | 2009-04-02 | 2011-09-22 | Roche Glycart Ag | Multispecific antibodies comprising full length antibodies and single chain Fab fragments |
| WO2011034605A2 (en) | 2009-09-16 | 2011-03-24 | Genentech, Inc. | Coiled coil and/or tether containing protein complexes and uses thereof |
| AR080793A1 (es) | 2010-03-26 | 2012-05-09 | Roche Glycart Ag | Anticuerpos biespecificos |
| JP5758004B2 (ja) | 2010-08-24 | 2015-08-05 | エフ．ホフマン−ラ ロシュ アーゲーＦ． Ｈｏｆｆｍａｎｎ−Ｌａ Ｒｏｃｈｅ Ａｋｔｉｅｎｇｅｓｅｌｌｓｃｈａｆｔ | ジスルフィドによって安定化されたＦｖ断片を含む二重特異性抗体 |
| SG191153A1 (en) | 2010-12-23 | 2013-07-31 | Hoffmann La Roche | Polypeptide-polynucleotide-complex and its use in targeted effector moiety delivery |
| WO2012115772A2 (en) | 2011-02-25 | 2012-08-30 | Medtronic, Inc. | Therapy for kidney disease and/or heart failure |
| ES2882852T3 (es) | 2011-03-16 | 2021-12-02 | Kuros Biosurgery Ag | Formulación farmacéutica para la utilización en la fusión espinal |
| WO2013033675A1 (en) | 2011-09-02 | 2013-03-07 | Medtronic, Inc. | Chimeric natriuretic peptide compositions and methods of preparation |
| JP6486686B2 (ja) | 2012-02-10 | 2019-03-20 | ジェネンテック， インコーポレイテッド | 単鎖抗体及び他のヘテロ多量体 |
| JP6309002B2 (ja) | 2012-06-27 | 2018-04-11 | エフ．ホフマン−ラ ロシュ アーゲーＦ． Ｈｏｆｆｍａｎｎ−Ｌａ Ｒｏｃｈｅ Ａｋｔｉｅｎｇｅｓｅｌｌｓｃｈａｆｔ | 標的に特異的に結合する少なくとも１つの結合実体を含む抗体Ｆｃ領域結合体を作製するための方法およびその使用 |
| CN110256567B (zh) | 2012-06-27 | 2023-04-25 | 弗·哈夫曼-拉罗切有限公司 | 用于选择并产生含有至少两种不同结合实体的定制靶向实体的方法及其用途 |
| US20140056870A1 (en) | 2012-08-27 | 2014-02-27 | Allergan, Inc. | Fusion proteins |
| CN107001482B (zh) | 2014-12-03 | 2021-06-15 | 豪夫迈·罗氏有限公司 | 多特异性抗体 |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0198015B2 (en) * | 1984-10-02 | 1995-07-19 | Biogen, Inc. | Production of streptavidin-like polypeptides |
| GB8518753D0 (en) * | 1985-07-24 | 1985-08-29 | Glaxo Group Ltd | Microbiological products |
| JP2819467B2 (ja) * | 1987-03-02 | 1998-10-30 | ファーマ・ビッセンドルフ・ペプタイド・ゲーエムベーハー | 新規なカルジオジラチン断片およびその製造方法 |
| GB8723661D0 (en) * | 1987-10-08 | 1987-11-11 | British Bio Technology | Synthetic gene |
| DE3935738A1 (de) * | 1989-10-27 | 1991-05-08 | Forssmann Wolf Georg | Arzneimittel, enthaltend das humane parathormon-fragment (1-37) als aktiven wirkstoff |
| ATE253639T1 (de) * | 1991-08-19 | 2003-11-15 | Daiichi Suntory Pharma Co Ltd | Verfahren zur herstellung von peptiden |
-
1996
- 1996-11-06 WO PCT/EP1996/004850 patent/WO1997018314A1/de not_active Ceased
- 1996-11-06 CA CA002237296A patent/CA2237296C/en not_active Expired - Fee Related
- 1996-11-06 AU AU75663/96A patent/AU7566396A/en not_active Abandoned
- 1996-11-06 US US09/068,738 patent/US6136564A/en not_active Expired - Fee Related
- 1996-11-06 JP JP9518551A patent/JP2000500019A/ja not_active Ceased
- 1996-11-06 EP EP96938115A patent/EP0861325A1/de not_active Withdrawn
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2005517658A (ja) * | 2001-12-18 | 2005-06-16 | エイドゲントシッシュ テクニーシェ ホッシュール チューリッヒ | 組織操作のための成長因子改変タンパク質マトリクス |
Also Published As
| Publication number | Publication date |
|---|---|
| US6136564A (en) | 2000-10-24 |
| AU7566396A (en) | 1997-06-05 |
| WO1997018314A1 (de) | 1997-05-22 |
| CA2237296A1 (en) | 1997-05-22 |
| CA2237296C (en) | 2008-10-07 |
| EP0861325A1 (de) | 1998-09-02 |
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