JPH0449999B2 - - Google Patents
Info
- Publication number
- JPH0449999B2 JPH0449999B2 JP58501024A JP50102483A JPH0449999B2 JP H0449999 B2 JPH0449999 B2 JP H0449999B2 JP 58501024 A JP58501024 A JP 58501024A JP 50102483 A JP50102483 A JP 50102483A JP H0449999 B2 JPH0449999 B2 JP H0449999B2
- Authority
- JP
- Japan
- Prior art keywords
- ifn
- human ifn
- solution
- sds
- butanol
- 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
- 238000000034 method Methods 0.000 description 53
- 101001054334 Homo sapiens Interferon beta Proteins 0.000 description 40
- BTANRVKWQNVYAZ-UHFFFAOYSA-N butan-2-ol Chemical group CCC(C)O BTANRVKWQNVYAZ-UHFFFAOYSA-N 0.000 description 36
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical group [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 28
- 239000000243 solution Substances 0.000 description 24
- 239000002904 solvent Substances 0.000 description 23
- 108090000623 proteins and genes Proteins 0.000 description 19
- 102000004169 proteins and genes Human genes 0.000 description 17
- 239000012736 aqueous medium Substances 0.000 description 16
- 244000005700 microbiome Species 0.000 description 16
- MSXVEPNJUHWQHW-UHFFFAOYSA-N 2-methylbutan-2-ol Chemical compound CCC(C)(C)O MSXVEPNJUHWQHW-UHFFFAOYSA-N 0.000 description 15
- 108090000467 Interferon-beta Proteins 0.000 description 15
- 210000004027 cell Anatomy 0.000 description 15
- 102100026720 Interferon beta Human genes 0.000 description 14
- 108010050904 Interferons Proteins 0.000 description 14
- 239000000284 extract Substances 0.000 description 14
- 102000014150 Interferons Human genes 0.000 description 13
- 241000588724 Escherichia coli Species 0.000 description 11
- 238000005063 solubilization Methods 0.000 description 11
- 230000007928 solubilization Effects 0.000 description 11
- 239000000203 mixture Substances 0.000 description 10
- LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 description 8
- 239000001963 growth medium Substances 0.000 description 8
- 229940079322 interferon Drugs 0.000 description 8
- 239000012071 phase Substances 0.000 description 8
- BTURAGWYSMTVOW-UHFFFAOYSA-M sodium dodecanoate Chemical compound [Na+].CCCCCCCCCCCC([O-])=O BTURAGWYSMTVOW-UHFFFAOYSA-M 0.000 description 8
- 229940082004 sodium laurate Drugs 0.000 description 8
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 7
- 210000000170 cell membrane Anatomy 0.000 description 7
- 230000000120 cytopathologic effect Effects 0.000 description 7
- 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 7
- 238000000605 extraction Methods 0.000 description 7
- 239000002953 phosphate buffered saline Substances 0.000 description 7
- 239000008346 aqueous phase Substances 0.000 description 6
- 238000003556 assay Methods 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 241000700605 Viruses Species 0.000 description 5
- 230000001413 cellular effect Effects 0.000 description 5
- 239000012141 concentrate Substances 0.000 description 5
- 229940047124 interferons Drugs 0.000 description 5
- 239000012074 organic phase Substances 0.000 description 5
- 239000002244 precipitate Substances 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 230000003612 virological effect Effects 0.000 description 5
- 241000894006 Bacteria Species 0.000 description 4
- 150000001298 alcohols Chemical class 0.000 description 4
- 229910052783 alkali metal Inorganic materials 0.000 description 4
- -1 alkali metal alkyl sulfate Chemical class 0.000 description 4
- 239000003945 anionic surfactant Substances 0.000 description 4
- 230000004071 biological effect Effects 0.000 description 4
- 239000003085 diluting agent Substances 0.000 description 4
- 239000012530 fluid Substances 0.000 description 4
- 238000002955 isolation Methods 0.000 description 4
- 239000007788 liquid Substances 0.000 description 4
- 239000002609 medium Substances 0.000 description 4
- 239000011236 particulate material Substances 0.000 description 4
- 239000011734 sodium Substances 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- QPRQEDXDYOZYLA-UHFFFAOYSA-N 2-methylbutan-1-ol Chemical compound CCC(C)CO QPRQEDXDYOZYLA-UHFFFAOYSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- YXFVVABEGXRONW-UHFFFAOYSA-N Toluene Chemical compound CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 239000007864 aqueous solution Substances 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 238000009826 distribution Methods 0.000 description 3
- 238000000855 fermentation Methods 0.000 description 3
- 230000004151 fermentation Effects 0.000 description 3
- 210000002950 fibroblast Anatomy 0.000 description 3
- 239000001257 hydrogen Substances 0.000 description 3
- 229910052739 hydrogen Inorganic materials 0.000 description 3
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 3
- 238000002156 mixing Methods 0.000 description 3
- 239000013618 particulate matter Substances 0.000 description 3
- 238000005191 phase separation Methods 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 239000000725 suspension Substances 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- KDCGOANMDULRCW-UHFFFAOYSA-N 7H-purine Chemical compound N1=CNC2=NC=NC2=C1 KDCGOANMDULRCW-UHFFFAOYSA-N 0.000 description 2
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 2
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- AMQJEAYHLZJPGS-UHFFFAOYSA-N N-Pentanol Chemical compound CCCCCO AMQJEAYHLZJPGS-UHFFFAOYSA-N 0.000 description 2
- 150000001413 amino acids Chemical group 0.000 description 2
- 239000012062 aqueous buffer Substances 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 125000004432 carbon atom Chemical group C* 0.000 description 2
- 239000006285 cell suspension Substances 0.000 description 2
- 230000001351 cycling effect Effects 0.000 description 2
- 235000014113 dietary fatty acids Nutrition 0.000 description 2
- 238000004090 dissolution Methods 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 229930195729 fatty acid Natural products 0.000 description 2
- 239000000194 fatty acid Substances 0.000 description 2
- 150000004665 fatty acids Chemical class 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- 238000003306 harvesting Methods 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 230000011542 interferon-beta production Effects 0.000 description 2
- 210000000265 leukocyte Anatomy 0.000 description 2
- 239000007791 liquid phase Substances 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 108020004999 messenger RNA Proteins 0.000 description 2
- 108020004707 nucleic acids Proteins 0.000 description 2
- 102000039446 nucleic acids Human genes 0.000 description 2
- 150000007523 nucleic acids Chemical class 0.000 description 2
- 229910001414 potassium ion Inorganic materials 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 229940071089 sarcosinate Drugs 0.000 description 2
- 229910052708 sodium Inorganic materials 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 230000003381 solubilizing effect Effects 0.000 description 2
- 238000000527 sonication Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- ZIIUUSVHCHPIQD-UHFFFAOYSA-N 2,4,6-trimethyl-N-[3-(trifluoromethyl)phenyl]benzenesulfonamide Chemical compound CC1=CC(C)=CC(C)=C1S(=O)(=O)NC1=CC=CC(C(F)(F)F)=C1 ZIIUUSVHCHPIQD-UHFFFAOYSA-N 0.000 description 1
- PFNHSEQQEPMLNI-UHFFFAOYSA-N 2-methyl-1-pentanol Substances CCCC(C)CO PFNHSEQQEPMLNI-UHFFFAOYSA-N 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- SNRUBQQJIBEYMU-UHFFFAOYSA-N Dodecane Natural products CCCCCCCCCCCC SNRUBQQJIBEYMU-UHFFFAOYSA-N 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 239000012981 Hank's balanced salt solution Substances 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 102000003996 Interferon-beta Human genes 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- 102000015439 Phospholipases Human genes 0.000 description 1
- 108010064785 Phospholipases Proteins 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- CZPWVGJYEJSRLH-UHFFFAOYSA-N Pyrimidine Chemical compound C1=CN=CN=C1 CZPWVGJYEJSRLH-UHFFFAOYSA-N 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
- 229960000583 acetic acid Drugs 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000002299 affinity electrophoresis Methods 0.000 description 1
- 125000003158 alcohol group Chemical group 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 239000007900 aqueous suspension Substances 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000007640 basal medium Substances 0.000 description 1
- 239000002585 base Substances 0.000 description 1
- 238000010364 biochemical engineering Methods 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000009295 crossflow filtration Methods 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 229940127089 cytotoxic agent Drugs 0.000 description 1
- 239000002254 cytotoxic agent Substances 0.000 description 1
- 231100000599 cytotoxic agent Toxicity 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- POULHZVOKOAJMA-UHFFFAOYSA-M dodecanoate Chemical compound CCCCCCCCCCCC([O-])=O POULHZVOKOAJMA-UHFFFAOYSA-M 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 238000005227 gel permeation chromatography Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000012362 glacial acetic acid Substances 0.000 description 1
- 238000000265 homogenisation Methods 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 229940070765 laurate Drugs 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 238000000622 liquid--liquid extraction Methods 0.000 description 1
- 239000011777 magnesium Substances 0.000 description 1
- 229910001425 magnesium ion Inorganic materials 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 239000002808 molecular sieve Substances 0.000 description 1
- 239000002106 nanomesh Substances 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 235000006180 nutrition needs Nutrition 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 238000010979 pH adjustment Methods 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 150000003904 phospholipids Chemical class 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000009703 regulation of cell differentiation Effects 0.000 description 1
- 230000021014 regulation of cell growth Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000002002 slurry Substances 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- URGAHOPLAPQHLN-UHFFFAOYSA-N sodium aluminosilicate Chemical compound [Na+].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O URGAHOPLAPQHLN-UHFFFAOYSA-N 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229910001415 sodium ion Inorganic materials 0.000 description 1
- 229940045845 sodium myristate Drugs 0.000 description 1
- 229960000776 sodium tetradecyl sulfate Drugs 0.000 description 1
- FIWQZURFGYXCEO-UHFFFAOYSA-M sodium;decanoate Chemical compound [Na+].CCCCCCCCCC([O-])=O FIWQZURFGYXCEO-UHFFFAOYSA-M 0.000 description 1
- XZTJQQLJJCXOLP-UHFFFAOYSA-M sodium;decyl sulfate Chemical compound [Na+].CCCCCCCCCCOS([O-])(=O)=O XZTJQQLJJCXOLP-UHFFFAOYSA-M 0.000 description 1
- DAJSVUQLFFJUSX-UHFFFAOYSA-M sodium;dodecane-1-sulfonate Chemical compound [Na+].CCCCCCCCCCCCS([O-])(=O)=O DAJSVUQLFFJUSX-UHFFFAOYSA-M 0.000 description 1
- JUQGWKYSEXPRGL-UHFFFAOYSA-M sodium;tetradecanoate Chemical compound [Na+].CCCCCCCCCCCCCC([O-])=O JUQGWKYSEXPRGL-UHFFFAOYSA-M 0.000 description 1
- UPUIQOIQVMNQAP-UHFFFAOYSA-M sodium;tetradecyl sulfate Chemical compound [Na+].CCCCCCCCCCCCCCOS([O-])(=O)=O UPUIQOIQVMNQAP-UHFFFAOYSA-M 0.000 description 1
- CACJZDMMUHMEBN-UHFFFAOYSA-M sodium;tridecane-1-sulfonate Chemical compound [Na+].CCCCCCCCCCCCCS([O-])(=O)=O CACJZDMMUHMEBN-UHFFFAOYSA-M 0.000 description 1
- 238000000638 solvent extraction Methods 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 230000003068 static effect Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 208000003265 stomatitis Diseases 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 229960003495 thiamine Drugs 0.000 description 1
- DPJRMOMPQZCRJU-UHFFFAOYSA-M thiamine hydrochloride Chemical compound Cl.[Cl-].CC1=C(CCO)SC=[N+]1CC1=CN=C(C)N=C1N DPJRMOMPQZCRJU-UHFFFAOYSA-M 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 229960004799 tryptophan Drugs 0.000 description 1
- 208000005925 vesicular stomatitis Diseases 0.000 description 1
- 238000005406 washing Methods 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/555—Interferons [IFN]
- C07K14/565—IFN-beta
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US353360 | 1982-03-01 | ||
| US06/353,360 US4450103A (en) | 1982-03-01 | 1982-03-01 | Process for recovering human IFN-β from a transformed microorganism |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS59500597A JPS59500597A (ja) | 1984-04-12 |
| JPH0449999B2 true JPH0449999B2 (enExample) | 1992-08-13 |
Family
ID=23388775
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP58501024A Granted JPS59500597A (ja) | 1982-03-01 | 1983-02-10 | 形質転換させた微生物からヒトＩＦＮ−βを回収する方法 |
Country Status (8)
| Country | Link |
|---|---|
| US (1) | US4450103A (enExample) |
| EP (1) | EP0102989B1 (enExample) |
| JP (1) | JPS59500597A (enExample) |
| AU (1) | AU549721B2 (enExample) |
| CA (1) | CA1187013A (enExample) |
| DE (1) | DE3363647D1 (enExample) |
| IT (1) | IT1164626B (enExample) |
| WO (1) | WO1983003103A1 (enExample) |
Families Citing this family (52)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4925919A (en) * | 1984-04-25 | 1990-05-15 | Roland Mertelsmann | Purified interleukin 2 |
| US5702699A (en) * | 1982-09-23 | 1997-12-30 | Cetus Corporation | Process for the recovery of lipophilic proteins |
| US4992271A (en) * | 1982-09-23 | 1991-02-12 | Cetus Corporation | Formulation for lipophilic IL-2 proteins |
| US4853332A (en) * | 1982-10-19 | 1989-08-01 | Cetus Corporation | Structural genes, plasmids and transformed cells for producing cysteine depleted muteins of biologically active proteins |
| JPS60118196A (ja) * | 1983-11-30 | 1985-06-25 | Takeda Chem Ind Ltd | インタ−フェロンの製造法 |
| US4530787A (en) * | 1984-03-28 | 1985-07-23 | Cetus Corporation | Controlled oxidation of microbially produced cysteine-containing proteins |
| US4569790A (en) * | 1984-03-28 | 1986-02-11 | Cetus Corporation | Process for recovering microbially produced interleukin-2 and purified recombinant interleukin-2 compositions |
| US4908434A (en) * | 1984-04-25 | 1990-03-13 | Sloan-Kettering Institute For Cancer Research | Process for preparing purified interleukin-2 |
| US4908433A (en) * | 1984-04-25 | 1990-03-13 | Sloan-Kettering Institute For Cancer Research | Uses of interleukin-2 |
| DE3421302A1 (de) * | 1984-06-08 | 1985-12-12 | Hoechst Ag, 6230 Frankfurt | Verfahren zur isolierung und reinigung von (alpha)-interferonen |
| US4572798A (en) * | 1984-12-06 | 1986-02-25 | Cetus Corporation | Method for promoting disulfide bond formation in recombinant proteins |
| US4748234A (en) * | 1985-06-26 | 1988-05-31 | Cetus Corporation | Process for recovering refractile bodies containing heterologous proteins from microbial hosts |
| US5248769A (en) * | 1985-06-26 | 1993-09-28 | Cetus Oncology Corporation | Process for recovering refractile bodies containing heterologous proteins from microbial hosts |
| US4675387A (en) | 1985-07-26 | 1987-06-23 | E. I. Du Pont De Nemours And Company | Method for extracting protein with organic acid |
| US4816440A (en) * | 1985-09-26 | 1989-03-28 | Cetus Corporation | Stable formulation of biologically active proteins for parenteral injection |
| US5183746A (en) * | 1986-10-27 | 1993-02-02 | Schering Aktiengesellschaft | Formulation processes for pharmaceutical compositions of recombinant β- |
| US5004605A (en) * | 1987-12-10 | 1991-04-02 | Cetus Corporation | Low pH pharmaceutical compositions of recombinant β-interferon |
| WO1992009623A1 (fr) * | 1990-11-23 | 1992-06-11 | Roussel-Uclaf | PROCEDE DE PREPARATION D'UNE PROTEINE COMPORTANT AU MOINS UN PONT DISULFURE INTRAMOLECULAIRE PAR OXYDATION, A UN pH INFERIEUR A 5,0, DE LA PROTEINE RECOMBINANTE REDUITE CORRESPONDANTE |
| DE4128319A1 (de) * | 1991-08-27 | 1993-03-04 | Bioferon Biochem Substanz | Neues rekombinantes human-ifn-beta, verfahren zu dessen herstellung und dieses enthaltende pharmazeutische zubereitungen |
| FR2686899B1 (fr) * | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| US6399296B1 (en) * | 1994-07-20 | 2002-06-04 | The General Hospital Corporation | Interaction trap systems for detecting protein interactions |
| DE69533144T2 (de) * | 1995-12-21 | 2004-11-11 | Genzyme Corp., Cambridge | Methode zur zellyse |
| US7026468B2 (en) * | 1996-07-19 | 2006-04-11 | Valentis, Inc. | Process and equipment for plasmid purification |
| US7807822B2 (en) | 1996-08-01 | 2010-10-05 | Robert Bridenbaugh | Methods for purifying nucleic acids |
| JP2001520889A (ja) | 1997-10-24 | 2001-11-06 | バレンティス，インコーポレイティド | ポリヌクレオチドトランスフェクション複合体を調製する方法 |
| JPH11335392A (ja) * | 1998-05-26 | 1999-12-07 | Hsp Kenkyusho:Kk | 可溶性タンパク質の回収方法 |
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Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4289689A (en) * | 1980-03-14 | 1981-09-15 | Hoffmann-La Roche Inc. | Preparation of homogeneous human fibroblast interferon |
| AU538665B2 (en) * | 1979-10-30 | 1984-08-23 | Juridical Foundation, Japanese Foundation For Cancer Research | Human interferon dna |
| GB2068970B (en) * | 1980-02-06 | 1983-06-22 | Searle & Co | Recombinant dna technique for the preparation of a protein resembling human interferon |
| DE3005897A1 (de) * | 1980-02-16 | 1981-09-03 | Hoechst Ag, 6000 Frankfurt | Genprodukt eines hoeheren organismus aus einem dieses gen enhtaltenden mikroorganismus |
| US4315852A (en) * | 1980-11-26 | 1982-02-16 | Schering Corporation | Extraction of interferon from bacteria |
-
1982
- 1982-03-01 US US06/353,360 patent/US4450103A/en not_active Expired - Lifetime
-
1983
- 1983-02-10 AU AU13317/83A patent/AU549721B2/en not_active Expired
- 1983-02-10 WO PCT/US1983/000177 patent/WO1983003103A1/en not_active Ceased
- 1983-02-10 EP EP83900886A patent/EP0102989B1/en not_active Expired
- 1983-02-10 DE DE8383900886T patent/DE3363647D1/de not_active Expired
- 1983-02-10 JP JP58501024A patent/JPS59500597A/ja active Granted
- 1983-02-17 CA CA000421837A patent/CA1187013A/en not_active Expired
- 1983-02-24 IT IT47779/83A patent/IT1164626B/it active
Also Published As
| Publication number | Publication date |
|---|---|
| EP0102989A1 (en) | 1984-03-21 |
| JPS59500597A (ja) | 1984-04-12 |
| EP0102989B1 (en) | 1986-05-28 |
| AU1331783A (en) | 1983-10-18 |
| IT8347779A0 (it) | 1983-02-24 |
| AU549721B2 (en) | 1986-02-06 |
| WO1983003103A1 (en) | 1983-09-15 |
| CA1187013A (en) | 1985-05-14 |
| DE3363647D1 (en) | 1986-07-03 |
| US4450103A (en) | 1984-05-22 |
| IT1164626B (it) | 1987-04-15 |
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