PL149079B1 - Method of obtaining polypeptides of ifn-beta type - Google Patents
Method of obtaining polypeptides of ifn-beta type Download PDFInfo
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- PL149079B1 PL149079B1 PL1981230484A PL23048481A PL149079B1 PL 149079 B1 PL149079 B1 PL 149079B1 PL 1981230484 A PL1981230484 A PL 1981230484A PL 23048481 A PL23048481 A PL 23048481A PL 149079 B1 PL149079 B1 PL 149079B1
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Classifications
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- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
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- 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
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
-
- 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
- C07K14/555—Interferons [IFN]
- C07K14/565—IFN-beta
-
- 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
- C12N15/52—Genes encoding for enzymes or proenzymes
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- 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
- 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
- C12N15/73—Expression systems using phage (lambda) regulatory sequences
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/40—Fusion polypeptide containing a tag for immunodetection, or an epitope for immunisation
-
- 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
-
- 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
- C12N2710/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA dsDNA viruses
- C12N2710/00011—Details
- C12N2710/22011—Polyomaviridae, e.g. polyoma, SV40, JC
- C12N2710/22022—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Biomedical Technology (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Wood Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Virology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Immunology (AREA)
- General Chemical & Material Sciences (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Saccharide Compounds (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
GB8011306 | 1980-04-03 | ||
GB8018701 | 1980-06-06 |
Publications (2)
Publication Number | Publication Date |
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PL230484A1 PL230484A1 (en) | 1983-07-18 |
PL149079B1 true PL149079B1 (en) | 1990-01-31 |
Family
ID=26275083
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PL1981230484A PL149079B1 (en) | 1980-04-03 | 1981-04-02 | Method of obtaining polypeptides of ifn-beta type |
Country Status (27)
Families Citing this family (41)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5554513A (en) * | 1979-11-21 | 1996-09-10 | Yeda Research & Development Co. Ltd. | Production of recombinant human interferon-beta2 |
IL58765A (en) * | 1979-11-21 | 1986-09-30 | Yeda Res & Dev | Process for the production of essentially pure messenger rna of human fibroblast interferon and process for the production of interferon beta |
US5510472A (en) * | 1979-11-21 | 1996-04-23 | Yeda Research And Development Co. Ltd. | Production of recombinant human interferon-beta2 |
DK33181A (da) * | 1980-02-06 | 1981-08-07 | Searle & Co | Fremgangsmaade til fremstilling af et interferonlignende protein |
DE3005843A1 (de) * | 1980-02-16 | 1981-09-10 | Hoechst Ag, 6000 Frankfurt | Genprodukt eines hoeheren organismus aus einem dieses gen enthaltenden mikroorganismus |
GR74282B (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) * | 1980-06-06 | 1984-06-21 | Biogen Nv | |
EP0042246B1 (en) * | 1980-06-12 | 1987-03-18 | The Cancer Institute Of Japanese Foundation For Cancer Research | Plasmid |
US4874702A (en) * | 1980-09-08 | 1989-10-17 | Biogen, Inc. | Vectors and methods for making such vectors and for expressive cloned genes |
NZ198445A (en) * | 1980-09-25 | 1984-05-31 | Genentech Inc | Production of human fibroblast interferon by recombinant dna technology |
ZA816621B (en) * | 1980-09-25 | 1982-09-29 | Genentech Inc | Microbial production of human fibroblast interferon |
IL63327A (en) * | 1981-07-16 | 1985-11-29 | Yeda Res & Dev | Production of interferon beta1 and alpha-phage recombinants for its production in host bacteria |
GB2108510B (en) * | 1981-10-03 | 1984-12-12 | Ciba Geigy Ag | Dnas, recombinant dnas, hosts containing them, polypeptides and processes for the production thereof |
JPS58110600A (ja) * | 1981-12-25 | 1983-07-01 | Kyowa Hakko Kogyo Co Ltd | ヒトβ型インタ−フエロン遺伝子を含む組みかえ体プラスミド |
JPS58141796A (ja) * | 1982-02-18 | 1983-08-23 | Kyowa Hakko Kogyo Co Ltd | ペプチドの製造法 |
US4582800A (en) * | 1982-07-12 | 1986-04-15 | Hoffmann-La Roche Inc. | Novel vectors and method for controlling interferon expression |
IL69382A (en) * | 1982-08-05 | 1991-01-31 | Carter William Alvin | Method of protecting plants against viral pathogens by inserting into plant cells genes encoding polypeptides containing interferon domains |
US4737462A (en) * | 1982-10-19 | 1988-04-12 | Cetus Corporation | Structural genes, plasmids and transformed cells for producing cysteine depleted muteins of interferon-β |
FI82266C (fi) * | 1982-10-19 | 1991-02-11 | Cetus Corp | Foerfarande foer framstaellning av il-2 -mutein. |
US4588585A (en) * | 1982-10-19 | 1986-05-13 | Cetus Corporation | Human recombinant cysteine depleted interferon-β muteins |
US4966843A (en) * | 1982-11-01 | 1990-10-30 | Cetus Corporation | Expression of interferon genes in Chinese hamster ovary cells |
GR79124B (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) * | 1982-12-22 | 1984-10-02 | Genentech Inc | |
GB8308235D0 (en) * | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
US4518584A (en) * | 1983-04-15 | 1985-05-21 | Cetus Corporation | Human recombinant interleukin-2 muteins |
DE3379506D1 (en) * | 1983-08-22 | 1989-05-03 | Kyowa Hakko Kogyo Kk | Process for producing peptide |
EP0226639B1 (en) * | 1985-05-29 | 1990-11-14 | The Green Cross Corporation | Process for preparing heterogenic protein |
WO1987000553A1 (en) * | 1985-07-16 | 1987-01-29 | The Green Cross Corporation | Process for preparing hetero-protein |
FR2635113B1 (fr) * | 1988-08-05 | 1992-07-24 | Sanofi Sa | Procede d'obtention d'interleukine-1 (beta) mature a partir de cellules d'e. coli transformees |
FR2686899B1 (fr) | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
US5545723A (en) * | 1994-03-15 | 1996-08-13 | Biogen Inc. | Muteins of IFN-β |
KR100711990B1 (ko) | 1997-09-23 | 2007-05-02 | 렌트슐러 비오테히놀로기 게엠베하 | 액상 인터페론-베타 제제 |
US7144574B2 (en) | 1999-08-27 | 2006-12-05 | Maxygen Aps | Interferon β variants and conjugates |
US6531122B1 (en) | 1999-08-27 | 2003-03-11 | Maxygen Aps | Interferon-β variants and conjugates |
US7431921B2 (en) | 1999-08-27 | 2008-10-07 | Maxygen Aps | Interferon beta-like molecules |
US6905688B2 (en) | 2000-04-12 | 2005-06-14 | Human Genome Sciences, Inc. | Albumin fusion proteins |
MXPA03007619A (es) | 2001-02-27 | 2003-12-04 | Maxygen Aps | Nuevas moleculas similares a interferon beta. |
PT1463751E (pt) | 2001-12-21 | 2013-08-26 | Human Genome Sciences Inc | Proteínas de fusão de albumina |
EP1594530A4 (en) | 2003-01-22 | 2006-10-11 | Human Genome Sciences Inc | HYBRID PROTEINS OF ALBUMIN |
JP2007519422A (ja) | 2004-02-02 | 2007-07-19 | アンブレツクス・インコーポレイテツド | 修飾されたヒト四螺旋バンドルポリペプチド及びそれらの使用 |
WO2008137471A2 (en) | 2007-05-02 | 2008-11-13 | Ambrx, Inc. | Modified interferon beta polypeptides and their uses |
DE102009032179A1 (de) | 2009-07-07 | 2011-01-13 | Biogenerix Ag | Verfahren zur Reinigung von Interferon beta |
Family Cites Families (82)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
DK1645C (da) | 1898-06-20 | Carl Christensen | Lommekniv med et i Skaftet indskydeligt Blad. | |
US3699222A (en) | 1958-03-11 | 1972-10-17 | Nat Res Dev | Production of viral interfering substances |
US4184917A (en) | 1974-04-01 | 1980-01-22 | Sandoz Ltd. | Process for producing a structurally modified interferon |
NL7404589A (nl) | 1974-04-03 | 1975-10-07 | Stichting Rega V Z W | Werkwijze voor het stabiliseren van interferon. |
GB1521032A (en) | 1974-08-08 | 1978-08-09 | Ici Ltd | Biological treatment |
US4237224A (en) | 1974-11-04 | 1980-12-02 | Board Of Trustees Of The Leland Stanford Jr. University | Process for producing biologically functional molecular chimeras |
FR2321298A1 (fr) * | 1975-08-01 | 1977-03-18 | Anvar | Procede de preparation de produits a activite interferon |
US4190495A (en) | 1976-09-27 | 1980-02-26 | Research Corporation | Modified microorganisms and method of preparing and using same |
US4264731A (en) | 1977-05-27 | 1981-04-28 | The Regents Of The University Of California | DNA Joining method |
DE2724918A1 (de) | 1977-06-02 | 1978-12-14 | Thomae Gmbh Dr K | Gewinnung und reinigung von humaninterferon |
CS215108B2 (en) | 1977-07-15 | 1982-07-30 | Wellcome Found | Method of making the interferrone |
ZA782933B (en) | 1977-09-23 | 1979-05-30 | Univ California | Purification of nucleotide sequences suitable for expression in bacteria |
US4283489A (en) | 1977-09-23 | 1981-08-11 | The Regents Of The University Of California | Purification of nucleotide sequences suitable for expression in bacteria |
IL55892A (en) | 1977-11-08 | 1983-10-31 | Genentech Inc | Cloning vehicle for transforming microbial host to render it capable of polypeptide expression,and products therefrom |
NZ188838A (en) | 1977-11-08 | 1982-09-14 | Genentech Inc | Dna coding for microbial expression of mammalian polypeptide recombinant microbial cloning vehicle |
BG38166A3 (bg) | 1977-11-08 | 1985-10-15 | Genentech, Inc. | Метод за получаване на полипептид,включващ експресия на негов хетероложен ген от рекомбинантен микробен клониращ вектор |
DE2759053A1 (de) | 1977-12-30 | 1979-07-12 | Uhlin | Verfahren zum herstellen von genprodukten von plasmid-dns |
FR2422956A1 (fr) | 1978-04-13 | 1979-11-09 | Pasteur Institut | Procede de detection et de caracterisation d'un acide nucleique ou d'une sequence de celui-ci, et reactif enzymatique pour la mise en oeuvre de ce procede |
DE2961658D1 (en) | 1978-05-17 | 1982-02-18 | Thomae Gmbh Dr K | Process for preparing human interferon |
US4322497A (en) | 1978-06-02 | 1982-03-30 | Eli Lilly And Company | Process for transducing Escherichia coli K12 χ1776 |
US4411994A (en) | 1978-06-08 | 1983-10-25 | The President And Fellows Of Harvard College | Protein synthesis |
US4307193A (en) | 1978-06-09 | 1981-12-22 | Toray Industries, Inc. | Method of producing interferon |
JPS5519239A (en) | 1978-07-28 | 1980-02-09 | Green Cross Corp:The | Interferon-producing attractant |
FI792481A7 (fi) | 1978-08-11 | 1981-01-01 | The Regents Of The Univ Of | Enkaroyyttisen proteiinin synteesi mikro-organismia käyttäen. |
JPS5561798A (en) | 1978-10-30 | 1980-05-09 | Noda Sangyo Kagaku Kenkyusho | Preparation of novel recombination dna |
JPS5564799A (en) | 1978-11-07 | 1980-05-15 | Toray Ind Inc | Multi-stage concentration and purification of interferon originated from human fibroblast |
US4241174A (en) | 1978-11-24 | 1980-12-23 | Hoffmann-La Roche Inc. | Interferon assay |
IN150740B (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1978-11-24 | 1982-12-04 | Hoffmann La Roche | |
NL8000127A (nl) | 1979-01-15 | 1980-07-17 | Harvard College | Werkwijze voor het vormen van prokaryotische of eukaryotische proteinen alsmede een daarbij toepasbaar gekoppeld gen. |
EP0014050A3 (en) | 1979-01-16 | 1980-10-01 | Beecham Group Plc | Interferon production |
US5326859A (en) * | 1979-10-30 | 1994-07-05 | Juridical Foundation, Japanese Foundation For Cancer Research | DNA and recombinant plasmid |
JPS56131598A (en) | 1980-03-19 | 1981-10-15 | Japan Found Cancer | Novel recombinant plasmid having gene of human fibroblastic interferon messenger rna |
US5514567A (en) | 1979-01-30 | 1996-05-07 | Juridical Foundation, Japanese Foundation For Cancer Research | DNA and recombinant plasmid |
JPS5663996A (en) | 1979-10-30 | 1981-05-30 | Japan Found Cancer | Novel recombinant having gene complementary to human interferon messenger rna |
US4357421A (en) | 1979-04-02 | 1982-11-02 | G. D. Searle & Co. | Synthetic gene coding for influenza hemagglutinin |
FI77877C (fi) | 1979-04-20 | 1989-05-10 | Technobiotic Ltd | Foerfarande foer framstaellning och rening av human le-formig interferonprotein. |
IL57108A (en) | 1979-04-22 | 1981-12-31 | Yeda Res & Dev | Assay for the quantitative determination of interferon and a kit therefor |
US4293652A (en) | 1979-05-25 | 1981-10-06 | Cetus Corporation | Method for synthesizing DNA sequentially |
GB2052516B (en) | 1979-06-01 | 1983-06-29 | Searle & Co | Plasmid vectors production and use thereof |
US4262090A (en) | 1979-06-04 | 1981-04-14 | Cetus Corporation | Interferon production |
WO1981000116A1 (en) | 1979-07-05 | 1981-01-22 | United States Res Corp | Method for the purification and analysis of interferon |
ZA803943B (en) | 1979-07-31 | 1981-06-24 | Hoffmann La Roche | Homogeneous fibroblast interferon and method for manufacture thereof |
JPS5651995A (en) | 1979-10-05 | 1981-05-09 | Green Cross Corp:The | Preparation of interferon |
NL7907791A (nl) | 1979-10-23 | 1981-04-27 | Stichting Rega V Z W | Werkwijze voor het zuiveren van interferon. |
AU538665B2 (en) * | 1979-10-30 | 1984-08-23 | Juridical Foundation, Japanese Foundation For Cancer Research | Human interferon dna |
IL58765A (en) * | 1979-11-21 | 1986-09-30 | Yeda Res & Dev | Process for the production of essentially pure messenger rna of human fibroblast interferon and process for the production of interferon beta |
EP0030094A1 (en) | 1979-11-30 | 1981-06-10 | Beecham Group Plc | Calcium enhanced interferon production process |
NZ195980A (en) | 1980-01-08 | 1984-10-19 | Biogen Nv | Dna sequences,recombinant dna molecules and processes for producing leukocyte interferon-like polypeptides;pharmaceutical and veterinary compositions |
DK33181A (da) | 1980-02-06 | 1981-08-07 | Searle & Co | Fremgangsmaade til fremstilling af et interferonlignende protein |
GB2068970B (en) * | 1980-02-06 | 1983-06-22 | Searle & Co | Recombinant dna technique for the preparation of a protein resembling human interferon |
IE51030B1 (en) | 1980-02-06 | 1986-09-17 | Searle & Co | Recombinant dna technique for the preparation of a protein resembling human interferon |
DE3005843A1 (de) | 1980-02-16 | 1981-09-10 | Hoechst Ag, 6000 Frankfurt | Genprodukt eines hoeheren organismus aus einem dieses gen enthaltenden mikroorganismus |
DE3005897A1 (de) | 1980-02-16 | 1981-09-03 | Hoechst Ag, 6000 Frankfurt | Genprodukt eines hoeheren organismus aus einem dieses gen enhtaltenden mikroorganismus |
JPS57500408A (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1980-02-25 | 1982-03-11 | ||
US4399216A (en) | 1980-02-25 | 1983-08-16 | The Trustees Of Columbia University | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
ZA811368B (en) | 1980-03-24 | 1982-04-28 | Genentech Inc | Bacterial polypedtide expression employing tryptophan promoter-operator |
US4338397A (en) | 1980-04-11 | 1982-07-06 | President And Fellows Of Harvard College | Mature protein synthesis |
DK220781A (da) | 1980-05-22 | 1981-11-23 | Deutsches Krebsforsch | Fremgangsmaade til fremstilling af interferon ii og stimulerede kloner til ydfoerelse af frmgangsmaaden |
DE3019621C2 (de) | 1980-05-22 | 1982-08-19 | Stiftung Deutsches Krebsforschungszentrum, 6900 Heidelberg | Verfahren zur Herstellung von Interferon II. |
JPS56167624A (en) | 1980-05-29 | 1981-12-23 | Toray Ind Inc | Method of interferon production |
JPS571237A (en) | 1980-06-03 | 1982-01-06 | Toshiba Corp | Combined integrared circuit device |
GR74282B (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1980-06-06 | 1984-06-21 | Biogen Nv | |
JPS575158A (en) | 1980-06-12 | 1982-01-11 | Matsushita Electric Works Ltd | Automatic resetting circuit for cpu function stopping phenomenon |
EP0042246B1 (en) * | 1980-06-12 | 1987-03-18 | The Cancer Institute Of Japanese Foundation For Cancer Research | Plasmid |
CH651308A5 (de) | 1980-07-01 | 1985-09-13 | Hoffmann La Roche | Interferone und deren herstellung. |
US4357422A (en) | 1980-08-14 | 1982-11-02 | Massachusetts Institute Of Technology | Method of enhancing interferon production |
US4874702A (en) | 1980-09-08 | 1989-10-17 | Biogen, Inc. | Vectors and methods for making such vectors and for expressive cloned genes |
NZ198445A (en) | 1980-09-25 | 1984-05-31 | Genentech Inc | Production of human fibroblast interferon by recombinant dna technology |
US4315852A (en) | 1980-11-26 | 1982-02-16 | Schering Corporation | Extraction of interferon from bacteria |
JPS58201794A (ja) | 1982-05-17 | 1983-11-24 | Toray Ind Inc | ヒトインターフェロンβの濃縮精製法 |
US4835256A (en) | 1982-09-30 | 1989-05-30 | New York University & Juridical Foundation | Human gamma interferon polypeptide having glutamine as the ninth n-terminal amino acid |
NZ210501A (en) | 1983-12-13 | 1991-08-27 | Kirin Amgen Inc | Erythropoietin produced by procaryotic or eucaryotic expression of an exogenous dna sequence |
AU594014B2 (en) | 1984-03-21 | 1990-03-01 | Research Corporation Technologies, Inc. | Recombinant DNA molecules |
NZ212207A (en) | 1984-05-31 | 1991-07-26 | Genentech Inc | Recombinant lymphotoxin |
EP0200425B1 (en) | 1985-04-22 | 1991-12-27 | Eli Lilly And Company | Recombinant dna expression vectors and dna compounds |
US4892819A (en) | 1985-11-25 | 1990-01-09 | Eli Lilly And Company | Recombinant DNA expression vectors and DNA compounds that encode isopenicillin N synthetase from penicillium chrysogenum |
EP0257994B1 (en) | 1986-08-29 | 1992-09-16 | Tonen Corporation | Dna coding for rinderpest virus antigen, its preparation and use |
DE3642096A1 (de) | 1986-12-10 | 1988-06-16 | Boehringer Ingelheim Int | Pferde-(gamma)-interferon |
EP0286114B1 (en) | 1987-04-09 | 1994-03-30 | SHIONOGI SEIYAKU KABUSHIKI KAISHA trading under the name of SHIONOGI & CO. LTD. | Reg gene and protein encoded by the gene |
ZA887773B (en) | 1987-10-26 | 1989-07-26 | Immunex Corp | Interleukin-7 |
US5258287A (en) | 1988-03-22 | 1993-11-02 | Genentech, Inc. | DNA encoding and methods of production of insulin-like growth factor binding protein BP53 |
JP3393180B2 (ja) | 1998-10-22 | 2003-04-07 | シャープ株式会社 | 半導体装置の製造方法 |
-
1981
- 1981-04-01 GR GR64561A patent/GR74498B/el unknown
- 1981-04-01 IN IN188/DEL/81A patent/IN156128B/en unknown
- 1981-04-01 FI FI811008A patent/FI88175C/fi not_active IP Right Cessation
- 1981-04-01 EP EP81301414A patent/EP0041313B1/en not_active Expired - Lifetime
- 1981-04-01 AU AU68979/81A patent/AU564690B2/en not_active Expired
- 1981-04-01 IE IE756/81A patent/IE57069B1/en not_active IP Right Cessation
- 1981-04-01 ES ES500966A patent/ES8302096A1/es not_active Expired
- 1981-04-01 NZ NZ196706A patent/NZ196706A/en unknown
- 1981-04-01 HU HU81841A patent/HU193507B/hu unknown
- 1981-04-01 YU YU859/81A patent/YU45104B/xx unknown
- 1981-04-01 DE DE8181301414T patent/DE3177213D1/de not_active Revoked
- 1981-04-01 CA CA374378A patent/CA1341604C/en active Active
- 1981-04-01 JP JP56047361A patent/JP2687995B2/ja not_active Expired - Lifetime
- 1981-04-01 AT AT81301414T patent/ATE56471T1/de active
- 1981-04-01 KR KR1019810001103A patent/KR860001471B1/ko not_active Expired
- 1981-04-01 PT PT72786A patent/PT72786B/pt unknown
- 1981-04-01 IL IL62552A patent/IL62552A0/xx unknown
- 1981-04-01 DK DK148581A patent/DK170476B1/da not_active IP Right Cessation
- 1981-04-01 NO NO811118A patent/NO811118L/no unknown
- 1981-04-02 PL PL1981230484A patent/PL149079B1/pl unknown
- 1981-04-02 DD DD81228897A patent/DD160280A5/de active IP Right Maintenance
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1985
- 1985-02-22 NO NO850735A patent/NO850735L/no unknown
- 1985-02-22 NO NO850734A patent/NO850734L/no unknown
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1992
- 1992-06-17 MX MX9202946A patent/MX9202946A/es unknown
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1994
- 1994-02-11 BG BG098456A patent/BG60441B2/bg unknown
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1995
- 1995-05-25 US US08/452,658 patent/US7635466B1/en active Active
- 1995-05-25 US US08/449,930 patent/US7588755B1/en active Active
- 1995-10-12 HK HK160095A patent/HK160095A/en not_active IP Right Cessation
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1997
- 1997-04-07 NL NL970018C patent/NL970018I1/nl unknown
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- 1997-09-03 LU LU90131C patent/LU90131I2/fr unknown
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