FI86886C - Nya expressionsplasmider och deras anvaendning i foerfarandet foer expressering av prokymosin koderande gen i e. coli - Google Patents
Nya expressionsplasmider och deras anvaendning i foerfarandet foer expressering av prokymosin koderande gen i e. coli Download PDFInfo
- Publication number
- FI86886C FI86886C FI840918A FI840918A FI86886C FI 86886 C FI86886 C FI 86886C FI 840918 A FI840918 A FI 840918A FI 840918 A FI840918 A FI 840918A FI 86886 C FI86886 C FI 86886C
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- FI
- Finland
- Prior art keywords
- plasmid
- dna
- ecori
- map shown
- prochymosin
- Prior art date
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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
- C12N9/6478—Aspartic endopeptidases (3.4.23)
- C12N9/6481—Pepsins (3.4.23.1; 3.4.23.2; 3.4.23.3)
-
- 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
- C07K1/1136—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 reversible modification of the secondary, tertiary or quarternary structure, e.g. using denaturating or stabilising agents
-
- 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
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/70—Vectors or expression systems specially adapted for E. coli
- C12N15/71—Expression systems using regulatory sequences derived from the trp-operon
-
- 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
- C12N9/6478—Aspartic endopeptidases (3.4.23)
- C12N9/6483—Chymosin (3.4.23.4), i.e. rennin
-
- 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)
- C12Y304/23—Aspartic endopeptidases (3.4.23)
- C12Y304/23004—Chymosin (3.4.23.4), i.e. rennin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
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- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Microbiology (AREA)
- Biophysics (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Crystallography & Structural Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Analytical Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Saccharide Compounds (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP58038439A JPS59166086A (ja) | 1983-03-09 | 1983-03-09 | 新規な発現型プラスミドとそれらを用いて仔牛プロキモシン遺伝子を大腸菌内で発現させる方法 |
| JP3843983 | 1983-03-09 |
Publications (4)
| Publication Number | Publication Date |
|---|---|
| FI840918A0 FI840918A0 (fi) | 1984-03-07 |
| FI840918L FI840918L (fi) | 1984-09-10 |
| FI86886B FI86886B (fi) | 1992-07-15 |
| FI86886C true FI86886C (fi) | 1992-10-26 |
Family
ID=12525334
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| FI840918A FI86886C (fi) | 1983-03-09 | 1984-03-07 | Nya expressionsplasmider och deras anvaendning i foerfarandet foer expressering av prokymosin koderande gen i e. coli |
Country Status (9)
| Country | Link |
|---|---|
| EP (1) | EP0121775A1 (enExample) |
| JP (1) | JPS59166086A (enExample) |
| AR (1) | AR241795A1 (enExample) |
| AU (1) | AU572827B2 (enExample) |
| BR (1) | BR8401049A (enExample) |
| DK (1) | DK136184A (enExample) |
| FI (1) | FI86886C (enExample) |
| IE (1) | IE57264B1 (enExample) |
| NZ (1) | NZ207414A (enExample) |
Families Citing this family (72)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0123928A3 (en) * | 1983-03-31 | 1986-02-05 | Codon Genetic Engineering Laboratories | Recombinant dna coding for a polypeptide displaying milk clotting activity |
| US4721673A (en) * | 1983-09-01 | 1988-01-26 | Genex Corporation | Recovery and activation process for microbially produced calf prochymosin |
| JPS60188077A (ja) * | 1984-03-09 | 1985-09-25 | Teruhiko Beppu | 仔牛プロキモシンｃＤΝＡの全配列を有する新規な発現プラスミド |
| JPS60188093A (ja) * | 1984-03-09 | 1985-09-25 | Teruhiko Beppu | 枯草菌に於ける形質発現プラスミド |
| US5082775A (en) * | 1984-05-11 | 1992-01-21 | Berlex Laboratories, Inc. | Efficient process for isolating insoluble heterologous protein using non-ionic detergents |
| US4705848A (en) * | 1986-06-02 | 1987-11-10 | International Minerals & Chemical Corp. | Isolation of bioactive, monomeric growth hormone |
| GB2200118A (en) * | 1987-01-23 | 1988-07-27 | Allelix Inc | Synthetic chymosin-and prochymosin-encoding DNA segments |
| ATE158816T1 (de) | 1990-11-26 | 1997-10-15 | Genetics Inst | Expression von pace in wirtszellen und verfahren zu dessen verwendung |
| US5629167A (en) | 1994-04-19 | 1997-05-13 | Biocine S.P.A. | Detection of antibodies against Chlamydia trachomatis pgp3 antigen in patient sera by enzyme-linked immunosorbent assay |
| CA2671261A1 (en) | 1997-11-06 | 1999-05-20 | Novartis Vaccines And Diagnostics S.R.L. | Neisserial antigens |
| EP1047784B2 (en) | 1998-01-14 | 2015-03-18 | Novartis Vaccines and Diagnostics S.r.l. | Neissera meningitidis antigens |
| GB9808932D0 (en) | 1998-04-27 | 1998-06-24 | Chiron Spa | Polyepitope carrier protein |
| EP2261338A3 (en) | 1998-05-01 | 2012-01-04 | Novartis Vaccines and Diagnostics, Inc. | Neisseria meningitidis antigens and compositions |
| WO2000066741A2 (en) | 1999-04-30 | 2000-11-09 | Chiron S.P.A. | Conserved neisserial antigens |
| GB9911683D0 (en) | 1999-05-19 | 1999-07-21 | Chiron Spa | Antigenic peptides |
| GB9916529D0 (en) | 1999-07-14 | 1999-09-15 | Chiron Spa | Antigenic peptides |
| JP2004508801A (ja) | 1999-10-29 | 2004-03-25 | カイロン ソチエタ ア レスポンサビリタ リミタータ | ナイセリア抗原性ペプチド |
| PT2289545T (pt) | 2000-01-17 | 2016-09-06 | Glaxosmithkline Biologicals Sa | Vacina de omv suplementada contra meningococos |
| CA2881568C (en) | 2000-10-27 | 2019-09-24 | Novartis Vaccines And Diagnostics, Inc. | Nucleic acids and proteins from streptococcus groups a & b |
| DK1334182T4 (da) | 2000-11-06 | 2021-04-26 | Eidgenoessische Technische Hochschule Eth | Fremgangsmåde til fremstilling af ikke-bovint chymosin og anvendelse heraf |
| GB0107658D0 (en) | 2001-03-27 | 2001-05-16 | Chiron Spa | Streptococcus pneumoniae |
| GB0107661D0 (en) | 2001-03-27 | 2001-05-16 | Chiron Spa | Staphylococcus aureus |
| ATE469915T1 (de) | 2001-07-27 | 2010-06-15 | Novartis Vaccines & Diagnostic | Antikörper gegen das meningokokken adhäsin app |
| RU2331435C2 (ru) | 2001-12-12 | 2008-08-20 | Чирон Срл. | Иммунизация против chlamydia trachomatis |
| AU2003243316A1 (en) | 2002-05-24 | 2003-12-12 | Nps Allelix Corp. | Method for enzymatic production of glp-2(1-33) and glp-2-(1-34) peptides |
| CA2485695A1 (en) | 2002-05-24 | 2003-12-04 | Fred W. Wagner | Method for universal enzymatic production of bioactive peptides |
| EP1562982B1 (en) | 2002-11-15 | 2010-05-05 | Novartis Vaccines and Diagnostics S.r.l. | Unexpected surface proteins in neisseria meningitidis |
| GB0227346D0 (en) | 2002-11-22 | 2002-12-31 | Chiron Spa | 741 |
| GB0308198D0 (en) | 2003-04-09 | 2003-05-14 | Chiron Srl | ADP-ribosylating bacterial toxin |
| US7348420B2 (en) | 2003-04-25 | 2008-03-25 | North Carolina State University | Lactobacillus acidophilus nucleic acid sequences encoding cell surface protein homologues and uses therefore |
| EP1651750B1 (en) | 2003-06-23 | 2011-04-06 | North Carolina State University | Lactobacillus acidophilus nucleic acids encoding fructo-oligosaccharide utilization compounds and uses thereof |
| HRP20120315T1 (hr) | 2003-11-21 | 2012-05-31 | Nps Pharmaceuticals | Proizvodnja peptida 2 nalik glukagonu i analoga |
| BRPI0507169A (pt) | 2004-02-02 | 2007-06-26 | Ambrx Inc | polipeptìdeos do hormÈnio de crescimento humano modificados e seu usos |
| US7459289B2 (en) | 2004-03-08 | 2008-12-02 | North Carolina State University | Lactobacillus acidophilus nucleic acid sequences encoding carbohydrate utilization-related proteins and uses therefor |
| US7632924B2 (en) | 2004-06-18 | 2009-12-15 | Ambrx, Inc. | Antigen-binding polypeptides and their uses |
| WO2006091231A2 (en) | 2004-07-21 | 2006-08-31 | Ambrx, Inc. | Biosynthetic polypeptides utilizing non-naturally encoded amino acids |
| BRPI0519430A2 (pt) | 2004-12-22 | 2009-02-10 | Ambrx Inc | hormânio do crescimento humano modificado |
| EP2399893B1 (en) | 2004-12-22 | 2018-08-15 | Ambrx, Inc. | Compositions containing, methods involving, and uses of non-natural amino acids and polypeptides |
| EP1871868A2 (en) | 2005-04-15 | 2008-01-02 | North Carolina State University | Methods and compositions to modulate adhesion and stress tolerance in bacteria |
| DK2339014T3 (en) | 2005-11-16 | 2015-07-20 | Ambrx Inc | Methods and compositions comprising non-natural amino acids |
| GB0524066D0 (en) | 2005-11-25 | 2006-01-04 | Chiron Srl | 741 ii |
| PT2054431E (pt) | 2006-06-09 | 2011-11-03 | Novartis Ag | Confórmeros de adesinas bacterianas |
| CN106008699A (zh) | 2006-09-08 | 2016-10-12 | Ambrx公司 | 经修饰的人类血浆多肽或Fc骨架和其用途 |
| CN107501407B (zh) | 2007-03-30 | 2022-03-18 | Ambrx公司 | 经修饰fgf-21多肽和其用途 |
| MX2010005317A (es) | 2007-11-20 | 2010-06-02 | Ambrx Inc | Polipeptidos de insulina modificados y sus usos. |
| MX344166B (es) | 2008-02-08 | 2016-12-07 | Ambrx Inc | Leptina-polipeptidos modificados y sus usos. |
| CN102356089B (zh) | 2008-02-21 | 2014-02-19 | 诺华股份有限公司 | 脑膜炎球菌fHBP多肽 |
| CN102159230A (zh) | 2008-07-23 | 2011-08-17 | Ambrx公司 | 经修饰的牛g-csf多肽和其用途 |
| AU2009296267B2 (en) | 2008-09-26 | 2013-10-31 | Ambrx, Inc. | Non-natural amino acid replication-dependent microorganisms and vaccines |
| BR122012024318A2 (pt) | 2008-09-26 | 2019-07-30 | Ambrx, Inc. | Polipeptídeos modificados de eritropoetina animal e seus usos |
| CN102596240B (zh) | 2009-08-27 | 2015-02-04 | 诺华股份有限公司 | 包括脑膜炎球菌fHBP序列的杂交多肽 |
| CA2779816A1 (en) | 2009-10-27 | 2011-05-05 | Novartis Ag | Modified meningococcal fhbp polypeptides |
| BR112012015597A2 (pt) | 2009-12-21 | 2017-01-31 | Ambrx Inc | peptídeos de somatotropina suínos modificados e seus usos |
| MX349301B (es) | 2009-12-21 | 2017-07-21 | Ambrx Inc | Polipéptidos de somatotropina bovina modificados y sus usos. |
| CN103221420A (zh) | 2010-05-19 | 2013-07-24 | 北卡罗莱纳州立大学 | 用于递送治疗性肽的组合物和方法 |
| US9567386B2 (en) | 2010-08-17 | 2017-02-14 | Ambrx, Inc. | Therapeutic uses of modified relaxin polypeptides |
| EA030886B1 (ru) | 2010-08-17 | 2018-10-31 | Амбркс, Инк. | Модифицированные полипептиды релаксина, содержащие некодируемую в природе аминокислоту, связанную с полимером, и их применение |
| TWI480288B (zh) | 2010-09-23 | 2015-04-11 | Lilly Co Eli | 牛顆粒細胞群落刺激因子及其變體之調配物 |
| RU2473683C1 (ru) * | 2011-12-15 | 2013-01-27 | Общество С Ограниченной Ответственностью "Фармапарк" | СПОСОБ ПРОМЫШЛЕННОГО КУЛЬТИВИРОВАНИЯ ШТАММОВ E.coli, ПОЛУЧЕННЫХ НА ОСНОВЕ ШТАММА BL21(DE3), НЕСУЩЕГО ГЕН T7 RNA ПОЛИМЕРАЗЫ ПОД КОНТРОЛЕМ lacUV5 ПРОМОТОРА, С ПОВЫШЕННЫМ СИНТЕЗОМ БИОМАССЫ И ВЫХОДОМ ЦЕЛЕВОГО БЕЛКА В ТЕЛЬЦАХ ВКЛЮЧЕНИЯ |
| WO2015059690A1 (en) | 2013-10-24 | 2015-04-30 | Yeda Research And Development Co. Ltd. | Polynucleotides encoding brex system polypeptides and methods of using s ame |
| CN114805532A (zh) | 2014-10-24 | 2022-07-29 | 百时美施贵宝公司 | 修饰的fgf-21多肽及其用途 |
| US10590426B2 (en) | 2016-08-22 | 2020-03-17 | Board Of Trustees Of Michigan State University | Genetic control of cell size |
| IL250479A0 (en) | 2017-02-06 | 2017-03-30 | Sorek Rotem | Genetically engineered cells expressing a disarm system that confers resistance to phages and methods for their production |
| PE20191716A1 (es) | 2017-02-08 | 2019-12-05 | Bristol Myers Squibb Co | Polipeptidos de relaxina modificada que comprenden un mejorador farmacocinetico y sus usos |
| CN107881162A (zh) * | 2017-12-25 | 2018-04-06 | 中诺生物科技发展江苏有限公司 | 一种工业化生产凝乳酶的方法 |
| IL258467A (en) | 2018-03-29 | 2018-07-04 | Ilana Kolodkin Gal | Methods of disrupting a biofilm and/or preventing formation of same |
| CA3111576A1 (en) | 2018-09-11 | 2020-03-19 | Ambrx, Inc. | Interleukin-2 polypeptide conjugates and their uses |
| WO2020202142A2 (en) | 2019-03-31 | 2020-10-08 | Yeda Research And Development Co. Ltd. | Anti-viral and anti-tumoral compounds |
| EP4117732A1 (en) | 2020-03-11 | 2023-01-18 | Ambrx, Inc. | Interleukin-2 polypeptide conjugates and methods of use thereof |
| EP4228656A4 (en) | 2020-08-18 | 2024-09-04 | Yeda Research and Development Co. Ltd | ANTI-VIRAL AND ANTI-TUMOR COMPOUNDS |
| IL288680A (en) | 2021-12-05 | 2023-07-01 | Yeda Res & Dev | Genetically modified phages and their use |
| WO2025215636A1 (en) | 2024-04-08 | 2025-10-16 | Yeda Research And Development Co. Ltd. | Anti-defense system polypeptides and uses thereof |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4666847A (en) * | 1981-01-16 | 1987-05-19 | Collaborative Research, Inc. | Recombinant DNA means and method |
| IE53517B1 (en) * | 1981-06-17 | 1988-12-07 | Celltech Ltd | Process for the production of a polypeptide |
| JPS589687A (ja) * | 1981-06-17 | 1983-01-20 | セルテク リミテッド | ポリペプチドの生産方法 |
| JPS5832896A (ja) * | 1981-08-24 | 1983-02-25 | Teruhiko Beppu | 複合プラスミド及びそれを含有する微生物 |
| BR8205954A (pt) * | 1981-10-14 | 1983-09-13 | Unilever Nv | Sequencia de dna,plasmidio recombinante,cultura bacteriana e microorganismos |
| ZA834095B (en) * | 1982-07-01 | 1984-02-29 | Genex Corp | Bovine calf chymosin |
| IE56372B1 (en) * | 1982-12-22 | 1991-07-03 | Genentech Inc | Microbially produced rennet methods for its production and plasmids used for its production |
-
1983
- 1983-03-09 JP JP58038439A patent/JPS59166086A/ja active Granted
-
1984
- 1984-02-29 DK DK136184A patent/DK136184A/da not_active Application Discontinuation
- 1984-03-07 FI FI840918A patent/FI86886C/fi not_active IP Right Cessation
- 1984-03-07 EP EP84102451A patent/EP0121775A1/en not_active Withdrawn
- 1984-03-07 NZ NZ207414A patent/NZ207414A/en unknown
- 1984-03-07 AU AU25357/84A patent/AU572827B2/en not_active Ceased
- 1984-03-08 IE IE559/84A patent/IE57264B1/en not_active IP Right Cessation
- 1984-03-08 BR BR8401049A patent/BR8401049A/pt unknown
- 1984-03-09 AR AR84295974A patent/AR241795A1/es active
Also Published As
| Publication number | Publication date |
|---|---|
| JPS6240999B2 (enExample) | 1987-09-01 |
| FI840918A0 (fi) | 1984-03-07 |
| AR241795A1 (es) | 1992-12-30 |
| FI840918L (fi) | 1984-09-10 |
| AU2535784A (en) | 1984-09-13 |
| BR8401049A (pt) | 1984-10-16 |
| DK136184A (da) | 1984-09-10 |
| IE840559L (en) | 1984-09-09 |
| EP0121775A1 (en) | 1984-10-17 |
| NZ207414A (en) | 1988-02-29 |
| IE57264B1 (en) | 1992-07-01 |
| JPS59166086A (ja) | 1984-09-19 |
| DK136184D0 (da) | 1984-02-29 |
| AU572827B2 (en) | 1988-05-19 |
| FI86886B (fi) | 1992-07-15 |
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Legal Events
| Date | Code | Title | Description |
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| MM | Patent lapsed |
Owner name: BEPPU, TERUHIKO |