JPH0771506B2 - 顆粒球−マクロファージコロニ−刺激因子の精製方法 - Google Patents
顆粒球−マクロファージコロニ−刺激因子の精製方法Info
- Publication number
- JPH0771506B2 JPH0771506B2 JP63105372A JP10537288A JPH0771506B2 JP H0771506 B2 JPH0771506 B2 JP H0771506B2 JP 63105372 A JP63105372 A JP 63105372A JP 10537288 A JP10537288 A JP 10537288A JP H0771506 B2 JPH0771506 B2 JP H0771506B2
- Authority
- JP
- Japan
- Prior art keywords
- csf
- glutathione
- microorganism
- folded
- solution
- 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 - Lifetime
Links
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 title claims abstract description 71
- 102000004457 Granulocyte-Macrophage Colony-Stimulating Factor Human genes 0.000 title claims abstract description 69
- 238000000034 method Methods 0.000 title claims abstract description 26
- 241000588724 Escherichia coli Species 0.000 claims abstract description 9
- 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 12
- 239000000203 mixture Substances 0.000 claims description 11
- 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
- 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
- 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 7
- 238000004587 chromatography analysis Methods 0.000 claims description 6
- 239000003638 chemical reducing agent Substances 0.000 claims description 5
- 239000003795 chemical substances by application Substances 0.000 claims description 5
- 239000000126 substance Substances 0.000 claims description 5
- 230000003196 chaotropic effect Effects 0.000 claims description 4
- 239000007791 liquid phase Substances 0.000 claims description 3
- 230000002934 lysing effect Effects 0.000 claims description 3
- 239000012071 phase Substances 0.000 claims description 3
- 238000004255 ion exchange chromatography Methods 0.000 claims description 2
- 238000002955 isolation Methods 0.000 abstract description 2
- 108090000623 proteins and genes Proteins 0.000 description 15
- 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
- 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 8
- 210000004027 cell Anatomy 0.000 description 7
- 239000013612 plasmid Substances 0.000 description 7
- 229940024606 amino acid Drugs 0.000 description 6
- 239000012634 fragment Substances 0.000 description 6
- 239000011780 sodium chloride Substances 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
- 230000004071 biological effect Effects 0.000 description 5
- 239000006228 supernatant Substances 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 4
- 241001460678 Napo <wasp> Species 0.000 description 4
- 239000003480 eluent Substances 0.000 description 4
- 239000013618 particulate matter Substances 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 108020004705 Codon Proteins 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
- 239000002299 complementary DNA Substances 0.000 description 3
- 239000002609 medium Substances 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
- 241000894006 Bacteria Species 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
- 239000007864 aqueous solution Substances 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 239000000356 contaminant Substances 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 238000000502 dialysis Methods 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
- 238000005342 ion exchange Methods 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 239000011236 particulate material Substances 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 230000035755 proliferation Effects 0.000 description 2
- 239000012465 retentate Substances 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 238000002741 site-directed mutagenesis Methods 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 238000000527 sonication Methods 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
- 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-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-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
- 239000004365 Protease Substances 0.000 description 1
- 238000010266 Sephadex chromatography Methods 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
- 208000007097 Urinary Bladder Neoplasms Diseases 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 238000007792 addition Methods 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000001185 bone marrow Anatomy 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
- 230000001413 cellular effect Effects 0.000 description 1
- 229940047120 colony stimulating factors Drugs 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 230000001351 cycling effect Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 239000003398 denaturant Substances 0.000 description 1
- 238000010586 diagram 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
- 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
- 239000013604 expression vector Substances 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
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000003394 haemopoietic effect Effects 0.000 description 1
- 238000000265 homogenisation Methods 0.000 description 1
- 102000046157 human CSF2 Human genes 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
- 239000002198 insoluble material Substances 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
- 239000006166 lysate Substances 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 239000013028 medium composition Substances 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
- 230000000813 microbial effect Effects 0.000 description 1
- 239000000479 mixture part Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 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
- 239000002953 phosphate buffered saline Substances 0.000 description 1
- 230000001376 precipitating effect Effects 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
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000004043 responsiveness Effects 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 238000000926 separation method 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
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 230000000476 thermogenic effect Effects 0.000 description 1
- 201000005112 urinary bladder cancer 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)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Biophysics (AREA)
- Medicinal Chemistry (AREA)
- Wood Science & Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- General Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Immunology (AREA)
- Microbiology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- General Engineering & Computer Science (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)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US4333187A | 1987-04-28 | 1987-04-28 | |
| US43331 | 1987-04-28 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS6427492A JPS6427492A (en) | 1989-01-30 |
| JPH0771506B2 true JPH0771506B2 (ja) | 1995-08-02 |
Family
ID=21926624
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP63105372A Expired - Lifetime JPH0771506B2 (ja) | 1987-04-28 | 1988-04-27 | 顆粒球−マクロファージコロニ−刺激因子の精製方法 |
Country Status (15)
| Country | Link |
|---|---|
| EP (1) | EP0289267B1 (en, 2012) |
| JP (1) | JPH0771506B2 (en, 2012) |
| KR (1) | KR960001740B1 (en, 2012) |
| AT (1) | ATE83780T1 (en, 2012) |
| AU (1) | AU621051B2 (en, 2012) |
| CA (1) | CA1302652C (en, 2012) |
| DE (1) | DE3876843T2 (en, 2012) |
| ES (1) | ES2036680T3 (en, 2012) |
| FI (1) | FI94867C (en, 2012) |
| GR (1) | GR3006984T3 (en, 2012) |
| IL (1) | IL86163A (en, 2012) |
| NO (1) | NO175638C (en, 2012) |
| NZ (1) | NZ224371A (en, 2012) |
| WO (1) | WO1988008428A1 (en, 2012) |
| ZA (1) | ZA882808B (en, 2012) |
Families Citing this family (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4929700A (en) * | 1987-04-16 | 1990-05-29 | Cetus Corporation | Production of purified, biologically active, bacterially produced recombinant human CSF-1 |
| CA1339757C (en) | 1987-04-16 | 1998-03-17 | Robert F. Halenbeck | Production of purified biologically active, bacterially produced recombinant human csf-1 |
| EP0719860B1 (en) * | 1988-05-13 | 2009-12-16 | Amgen Inc. | Process for isolating and purifying G-CSF |
| 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 |
| US8161889B2 (en) | 2006-11-16 | 2012-04-24 | Mitsubishi Heavy Industries, Ltd. | Bogie structure for a track vehicle |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GR79124B (en, 2012) * | 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 |
| CN1031465C (zh) * | 1984-11-20 | 1996-04-03 | 先灵生物技术公司 | 编码表现有人粒细胞巨口噬细胞和嗜伊红细胞生长因子活性多之肽cDNA克隆 |
| 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 WO PCT/US1988/001228 patent/WO1988008428A1/en active IP Right Grant
- 1988-04-19 AU AU17115/88A patent/AU621051B2/en not_active Expired
- 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 ES ES198888303757T patent/ES2036680T3/es not_active Expired - Lifetime
- 1988-04-26 EP EP88303757A patent/EP0289267B1/en not_active Expired - Lifetime
- 1988-04-26 DE DE8888303757T patent/DE3876843T2/de not_active Expired - Fee Related
- 1988-04-26 NZ NZ224371A patent/NZ224371A/en unknown
- 1988-04-26 AT AT88303757T patent/ATE83780T1/de active
- 1988-04-27 CA CA000565271A patent/CA1302652C/en not_active Expired - Lifetime
- 1988-04-27 JP JP63105372A patent/JPH0771506B2/ja 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
Non-Patent Citations (1)
| Title |
|---|
| Ｂｌｏｏｄ，Ｖｏｌ．６９，Ｎｏ．１（１９８７．１）Ｐ．４３−５１ |
Also Published As
| Publication number | Publication date |
|---|---|
| EP0289267B1 (en) | 1992-12-23 |
| KR890701616A (ko) | 1989-12-21 |
| KR960001740B1 (en) | 1996-02-05 |
| NO175638C (no) | 1994-11-09 |
| NZ224371A (en) | 1990-11-27 |
| CA1302652C (en) | 1992-06-02 |
| EP0289267A2 (en) | 1988-11-02 |
| DE3876843T2 (de) | 1993-04-29 |
| EP0289267A3 (en) | 1989-11-08 |
| ZA882808B (en) | 1988-10-20 |
| JPS6427492A (en) | 1989-01-30 |
| ATE83780T1 (de) | 1993-01-15 |
| IL86163A (en) | 1992-11-15 |
| DE3876843D1 (de) | 1993-02-04 |
| AU1711588A (en) | 1988-12-02 |
| WO1988008428A1 (en) | 1988-11-03 |
| NO175638B (en, 2012) | 1994-08-01 |
| AU621051B2 (en) | 1992-03-05 |
| GR3006984T3 (en, 2012) | 1993-06-30 |
| ES2036680T3 (es) | 1993-06-01 |
| NO885777D0 (no) | 1988-12-27 |
| FI885986L (fi) | 1988-12-27 |
| NO885777L (no) | 1988-12-27 |
| FI94867C (fi) | 1995-11-10 |
| FI94867B (fi) | 1995-07-31 |
| IL86163A0 (en) | 1988-11-15 |
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Legal Events
| Date | Code | Title | Description |
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