NO175638B - - Google Patents

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Info

Publication number: NO175638B
Authority: NO; Norway
Prior art keywords: csf; solution; oxidized; glutathione; microorganism
Prior art date: 1987-04-28

Application number

NO885777A

Other languages

English (en)

Norwegian (no)

Other versions

NO175638C (no

NO885777D0 (no

NO885777L (no

Priority date (The priority date 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 date listed.)

1987-04-28

Filing date

1988-12-27

Publication date

1994-08-01

1988-12-27 Application filed filed Critical

1988-12-27 Publication of NO885777D0 publication Critical patent/NO885777D0/no

1988-12-27 Publication of NO885777L publication Critical patent/NO885777L/no

1994-08-01 Publication of NO175638B publication Critical patent/NO175638B/no

1994-11-09 Publication of NO175638C publication Critical patent/NO175638C/no

Links

238000000034 method Methods 0.000 claims abstract description 27
241000588724 Escherichia coli Species 0.000 claims abstract description 8
102000004457 Granulocyte-Macrophage Colony-Stimulating Factor Human genes 0.000 claims abstract 24
108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 claims abstract 24
RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 claims description 20
244000005700 microbiome Species 0.000 claims description 17
239000000203 mixture Substances 0.000 claims description 13
108010024636 Glutathione Proteins 0.000 claims description 10
229960003180 glutathione Drugs 0.000 claims description 10
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 claims description 9
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 8
239000004202 carbamide Substances 0.000 claims description 8
YPZRWBKMTBYPTK-UHFFFAOYSA-N oxidized gamma-L-glutamyl-L-cysteinylglycine Natural products OC(=O)C(N)CCC(=O)NC(C(=O)NCC(O)=O)CSSCC(C(=O)NCC(O)=O)NC(=O)CCC(N)C(O)=O YPZRWBKMTBYPTK-UHFFFAOYSA-N 0.000 claims description 8
108010053070 Glutathione Disulfide Proteins 0.000 claims description 7
YPZRWBKMTBYPTK-BJDJZHNGSA-N glutathione disulfide Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(=O)NCC(O)=O)CSSC[C@@H](C(=O)NCC(O)=O)NC(=O)CC[C@H](N)C(O)=O YPZRWBKMTBYPTK-BJDJZHNGSA-N 0.000 claims description 7
239000002198 insoluble material Substances 0.000 claims description 7
230000001105 regulatory effect Effects 0.000 claims description 7
239000003638 chemical reducing agent Substances 0.000 claims description 5
239000003795 chemical substances by application Substances 0.000 claims description 5
230000003196 chaotropic effect Effects 0.000 claims description 4
239000000463 material Substances 0.000 claims description 4
238000004128 high performance liquid chromatography Methods 0.000 claims description 2
238000004255 ion exchange chromatography Methods 0.000 claims description 2
238000001556 precipitation Methods 0.000 claims description 2
230000014759 maintenance of location Effects 0.000 claims 1
238000002955 isolation Methods 0.000 abstract description 2
108090000623 proteins and genes Proteins 0.000 description 16
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 14
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 12
102000004169 proteins and genes Human genes 0.000 description 12
239000000243 solution Substances 0.000 description 12
239000007983 Tris buffer Substances 0.000 description 9
210000004027 cell Anatomy 0.000 description 9
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 9
150000001413 amino acids Chemical group 0.000 description 7
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
239000012634 fragment Substances 0.000 description 6
239000013618 particulate matter Substances 0.000 description 6
239000013612 plasmid Substances 0.000 description 6
239000011780 sodium chloride Substances 0.000 description 6
108020004414 DNA Proteins 0.000 description 5
230000004071 biological effect Effects 0.000 description 5
239000003480 eluent Substances 0.000 description 5
239000006228 supernatant Substances 0.000 description 5
229940024606 amino acid Drugs 0.000 description 4
238000000746 purification Methods 0.000 description 4
108020004705 Codon Proteins 0.000 description 3
241001460678 Napo <wasp> Species 0.000 description 3
108091034117 Oligonucleotide Proteins 0.000 description 3
229920002684 Sepharose Polymers 0.000 description 3
VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 3
238000012986 modification Methods 0.000 description 3
230000004048 modification Effects 0.000 description 3
239000006176 redox buffer Substances 0.000 description 3
108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 2
102000003886 Glycoproteins Human genes 0.000 description 2
108090000288 Glycoproteins Proteins 0.000 description 2
241001625930 Luria Species 0.000 description 2
102000035195 Peptidases Human genes 0.000 description 2
108091005804 Peptidases Proteins 0.000 description 2
102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
238000005119 centrifugation Methods 0.000 description 2
239000002299 complementary DNA Substances 0.000 description 2
239000000356 contaminant Substances 0.000 description 2
239000003398 denaturant Substances 0.000 description 2
239000013613 expression plasmid Substances 0.000 description 2
239000013604 expression vector Substances 0.000 description 2
239000012467 final product Substances 0.000 description 2
PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 2
238000000265 homogenisation Methods 0.000 description 2
238000005342 ion exchange Methods 0.000 description 2
239000012528 membrane Substances 0.000 description 2
239000012071 phase Substances 0.000 description 2
239000012465 retentate Substances 0.000 description 2
238000000926 separation method Methods 0.000 description 2
238000002741 site-directed mutagenesis Methods 0.000 description 2
239000002904 solvent Substances 0.000 description 2
239000013598 vector Substances 0.000 description 2
206010005003 Bladder cancer Diseases 0.000 description 1
108091026890 Coding region Proteins 0.000 description 1
102000007644 Colony-Stimulating Factors Human genes 0.000 description 1
108010071942 Colony-Stimulating Factors Proteins 0.000 description 1
229920002271 DEAE-Sepharose Polymers 0.000 description 1
102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 description 1
108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 description 1
101000746373 Homo sapiens Granulocyte-macrophage colony-stimulating factor Proteins 0.000 description 1
AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
102000007651 Macrophage Colony-Stimulating Factor Human genes 0.000 description 1
108010046938 Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
241000276498 Pollachius virens Species 0.000 description 1
239000004365 Protease Substances 0.000 description 1
229920005654 Sephadex Polymers 0.000 description 1
239000012507 Sephadex™ Substances 0.000 description 1
VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
108020005038 Terminator Codon Proteins 0.000 description 1
AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
239000004473 Threonine Substances 0.000 description 1
239000002253 acid Substances 0.000 description 1
239000011149 active material Substances 0.000 description 1
238000007792 addition Methods 0.000 description 1
239000002671 adjuvant Substances 0.000 description 1
230000002411 adverse Effects 0.000 description 1
239000007864 aqueous solution Substances 0.000 description 1
230000015572 biosynthetic process Effects 0.000 description 1
210000004369 blood Anatomy 0.000 description 1
239000008280 blood Substances 0.000 description 1
239000000872 buffer Substances 0.000 description 1
229940041514 candida albicans extract Drugs 0.000 description 1
239000013592 cell lysate Substances 0.000 description 1
210000000170 cell membrane Anatomy 0.000 description 1
238000004587 chromatography analysis Methods 0.000 description 1
230000001684 chronic effect Effects 0.000 description 1
229940047120 colony stimulating factors Drugs 0.000 description 1
239000000470 constituent Substances 0.000 description 1
238000010276 construction Methods 0.000 description 1
239000012228 culture supernatant Substances 0.000 description 1
238000012217 deletion Methods 0.000 description 1
230000037430 deletion Effects 0.000 description 1
238000000502 dialysis Methods 0.000 description 1
LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
239000012636 effector Substances 0.000 description 1
230000000694 effects Effects 0.000 description 1
238000010828 elution Methods 0.000 description 1
210000003979 eosinophil Anatomy 0.000 description 1
230000000925 erythroid effect Effects 0.000 description 1
DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
238000000855 fermentation Methods 0.000 description 1
230000004151 fermentation Effects 0.000 description 1
238000001914 filtration Methods 0.000 description 1
230000005714 functional activity Effects 0.000 description 1
239000000499 gel Substances 0.000 description 1
210000003714 granulocyte Anatomy 0.000 description 1
239000001963 growth medium Substances 0.000 description 1
230000003394 haemopoietic effect Effects 0.000 description 1
102000046157 human CSF2 Human genes 0.000 description 1
238000009396 hybridization Methods 0.000 description 1
239000001257 hydrogen Substances 0.000 description 1
229910052739 hydrogen Inorganic materials 0.000 description 1
238000000338 in vitro Methods 0.000 description 1
210000003000 inclusion body Anatomy 0.000 description 1
229960000310 isoleucine Drugs 0.000 description 1
AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
238000011031 large-scale manufacturing process Methods 0.000 description 1
125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
239000007791 liquid phase Substances 0.000 description 1
239000006166 lysate Substances 0.000 description 1
210000004962 mammalian cell Anatomy 0.000 description 1
238000004519 manufacturing process Methods 0.000 description 1
229930182817 methionine Natural products 0.000 description 1
125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
210000001616 monocyte Anatomy 0.000 description 1
230000007935 neutral effect Effects 0.000 description 1
210000000440 neutrophil Anatomy 0.000 description 1
235000015097 nutrients Nutrition 0.000 description 1
239000002953 phosphate buffered saline Substances 0.000 description 1
239000002244 precipitate Substances 0.000 description 1
239000002243 precursor Substances 0.000 description 1
238000002360 preparation method Methods 0.000 description 1
229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
230000008707 rearrangement Effects 0.000 description 1
238000012163 sequencing technique Methods 0.000 description 1
239000000741 silica gel Substances 0.000 description 1
229910002027 silica gel Inorganic materials 0.000 description 1
239000000377 silicon dioxide Substances 0.000 description 1
239000001632 sodium acetate Substances 0.000 description 1
235000017281 sodium acetate Nutrition 0.000 description 1
230000007928 solubilization Effects 0.000 description 1
238000005063 solubilization Methods 0.000 description 1
238000000527 sonication Methods 0.000 description 1
238000006467 substitution reaction Methods 0.000 description 1
239000000725 suspension Substances 0.000 description 1
230000001225 therapeutic effect Effects 0.000 description 1
208000010570 urinary bladder carcinoma Diseases 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
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- 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
- C07K14/53—Colony-stimulating factor [CSF]
- C07K14/535—Granulocyte CSF; Granulocyte-macrophage CSF
- 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

Landscapes

Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Molecular Biology (AREA)
General Health & Medical Sciences (AREA)
Zoology (AREA)
Biochemistry (AREA)
Genetics & Genomics (AREA)
Engineering & Computer Science (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Medicinal Chemistry (AREA)
Biophysics (AREA)
Wood Science & Technology (AREA)
General Chemical & Material Sciences (AREA)
Chemical Kinetics & Catalysis (AREA)
Bioinformatics & Cheminformatics (AREA)
Immunology (AREA)
Toxicology (AREA)
Gastroenterology & Hepatology (AREA)
Microbiology (AREA)
General Engineering & Computer Science (AREA)
Biotechnology (AREA)
Analytical Chemistry (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Peptides Or Proteins (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)

NO885777A 1987-04-28 1988-12-27 Fremgangsmåte for isolering av granulocytt/makrofag-kolonistimulerende faktor (GM-CSF) fra en GM-CSF-produserende mikroorganisme NO175638C (no)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US4333187A	1987-04-28	1987-04-28
PCT/US1988/001228 WO1988008428A1 (en)	1987-04-28	1988-04-19	Method for purifying granulocyte/macrophage colony stimulating factor

Publications (4)

Publication Number	Publication Date
NO885777D0 NO885777D0 (no)	1988-12-27
NO885777L NO885777L (no)	1988-12-27
NO175638B true NO175638B (de)	1994-08-01
NO175638C NO175638C (no)	1994-11-09

Family

ID=21926624

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
NO885777A NO175638C (no)	1987-04-28	1988-12-27	Fremgangsmåte for isolering av granulocytt/makrofag-kolonistimulerende faktor (GM-CSF) fra en GM-CSF-produserende mikroorganisme

Country Status (15)

Country	Link
EP (1)	EP0289267B1 (de)
JP (1)	JPH0771506B2 (de)
KR (1)	KR960001740B1 (de)
AT (1)	ATE83780T1 (de)
AU (1)	AU621051B2 (de)
CA (1)	CA1302652C (de)
DE (1)	DE3876843T2 (de)
ES (1)	ES2036680T3 (de)
FI (1)	FI94867C (de)
GR (1)	GR3006984T3 (de)
IL (1)	IL86163A (de)
NO (1)	NO175638C (de)
NZ (1)	NZ224371A (de)
WO (1)	WO1988008428A1 (de)
ZA (1)	ZA882808B (de)

Families Citing this family (7)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CA1339757C (en) *	1987-04-16	1998-03-17	Robert F. Halenbeck	Production of purified biologically active, bacterially produced recombinant human csf-1
US4929700A (en) *	1987-04-16	1990-05-29	Cetus Corporation	Production of purified, biologically active, bacterially produced recombinant human CSF-1
FI900178A0 (fi) *	1988-05-13	1990-01-12	Amgen Inc	Kompositioner och foerfarande foer behandling eller foerhindrande av infektioner hos djur.
JP2517100B2 (ja) *	1989-03-08	1996-07-24	協和醗酵工業株式会社	ヒト顆粒球コロニ―刺激因子活性を有する蛋白質の精製法
GB9107846D0 (en) *	1990-04-30	1991-05-29	Ici Plc	Polypeptides
US6911204B2 (en)	2000-08-11	2005-06-28	Favrille, Inc.	Method and composition for altering a B cell mediated pathology
WO2008059604A1 (en)	2006-11-16	2008-05-22	Mitsubishi Heavy Industries, Ltd.	Truck structure of track-type vehicle

Family Cites Families (7)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
GR79124B (de) *	1982-12-22	1984-10-02	Genentech Inc
US4530787A (en) *	1984-03-28	1985-07-23	Cetus Corporation	Controlled oxidation of microbially produced cysteine-containing proteins
EP0202300B1 (de) *	1984-11-20	1992-11-11	Schering Biotech Corporation	Cdna-klone, kodierend für peptide mit der wirksamkeit eines menschlichen granulocyte-, makrophage- und eosinophilzellenwachstumsfaktors
GB8508340D0 (en) *	1985-03-29	1985-05-09	Creighton T E	Production of protein
US4748234A (en) *	1985-06-26	1988-05-31	Cetus Corporation	Process for recovering refractile bodies containing heterologous proteins from microbial hosts
DE3537708A1 (de) *	1985-10-23	1987-04-23	Boehringer Mannheim Gmbh	Verfahren zur aktivierung von t-pa nach expression in prokaryonten
US4734362A (en) *	1986-02-03	1988-03-29	Cambridge Bioscience Corporation	Process for purifying recombinant proteins, and products thereof

1988
- 1988-04-19 AU AU17115/88A patent/AU621051B2/en not_active Expired
- 1988-04-19 WO PCT/US1988/001228 patent/WO1988008428A1/en not_active Ceased
- 1988-04-21 ZA ZA882808A patent/ZA882808B/xx unknown
- 1988-04-25 IL IL86163A patent/IL86163A/xx not_active IP Right Cessation
- 1988-04-26 DE DE8888303757T patent/DE3876843T2/de not_active Expired - Fee Related
- 1988-04-26 EP EP88303757A patent/EP0289267B1/de not_active Expired - Lifetime
- 1988-04-26 NZ NZ224371A patent/NZ224371A/en unknown
- 1988-04-26 AT AT88303757T patent/ATE83780T1/de active
- 1988-04-26 ES ES198888303757T patent/ES2036680T3/es not_active Expired - Lifetime
- 1988-04-27 JP JP63105372A patent/JPH0771506B2/ja not_active Expired - Lifetime
- 1988-04-27 CA CA000565271A patent/CA1302652C/en not_active Expired - Lifetime
- 1988-12-27 NO NO885777A patent/NO175638C/no unknown
- 1988-12-27 FI FI885986A patent/FI94867C/fi not_active IP Right Cessation
- 1988-12-28 KR KR88701747A patent/KR960001740B1/ko not_active Expired - Lifetime
1993
- 1993-02-04 GR GR930400234T patent/GR3006984T3/el unknown

Also Published As

Publication number	Publication date
JPS6427492A (en)	1989-01-30
DE3876843D1 (de)	1993-02-04
NZ224371A (en)	1990-11-27
KR960001740B1 (en)	1996-02-05
NO175638C (no)	1994-11-09
FI94867B (fi)	1995-07-31
DE3876843T2 (de)	1993-04-29
GR3006984T3 (de)	1993-06-30
FI885986L (fi)	1988-12-27
WO1988008428A1 (en)	1988-11-03
ATE83780T1 (de)	1993-01-15
KR890701616A (ko)	1989-12-21
AU1711588A (en)	1988-12-02
NO885777D0 (no)	1988-12-27
FI94867C (fi)	1995-11-10
IL86163A0 (en)	1988-11-15
AU621051B2 (en)	1992-03-05
ES2036680T3 (es)	1993-06-01
EP0289267A2 (de)	1988-11-02
CA1302652C (en)	1992-06-02
EP0289267B1 (de)	1992-12-23
ZA882808B (en)	1988-10-20
IL86163A (en)	1992-11-15
EP0289267A3 (en)	1989-11-08
NO885777L (no)	1988-12-27
JPH0771506B2 (ja)	1995-08-02

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EP0818466B1 (de)	2005-08-03	Gereinigter, biologisch aktiver, bakteriell produzierter, rekombinanter humaner CSF-1.
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US5055555A (en)	1991-10-08	Purification of G-CSF
US5272254A (en)	1993-12-21	Production of streptavidin-like polypeptides
HUT56134A (en)	1991-07-29	Process for producing and purifying recombinant human interleukin-3 and its muteins
CA1302652C (en)	1992-06-02	Method for purifying granulocyte-macrophage colony stimulating factor
CA1339757C (en)	1998-03-17	Production of purified biologically active, bacterially produced recombinant human csf-1
US5047504A (en)	1991-09-10	Method for purifying granulocyte-macrophage colony stimulating factor
AU2011209506A1 (en)	2012-08-23	Method for producing interferon alpha 5
PT92335A (pt)	1990-05-31	Processo para a preparacao de proteinas hibridas da interleucemia -2 recombinante e de composicoes farmaceuticas que as contem
EP0315950A2 (de)	1989-05-17	Verfahren zur Züchtung von Zellen, welche rekombinantes Protein exprimieren
JP3004788B2 (ja)	2000-01-31	アルギニンデイミナーゼ発現ベクター、形質転換微生物およびアルギニンデイミナーゼの製造法
EP0423641A2 (de)	1991-04-24	Expressionsvektor, transformierter Mikroorganismus, Fusionsprotein und Verfahren zur Herstellung von Plättchen Faktor 4 oder TgF-alpha
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