HU197357B - Process for cleaning and reactivating precipitated heterologous proteins - Google Patents
Process for cleaning and reactivating precipitated heterologous proteins Download PDFInfo
- Publication number
- HU197357B HU197357B HU834379A HU437983A HU197357B HU 197357 B HU197357 B HU 197357B HU 834379 A HU834379 A HU 834379A HU 437983 A HU437983 A HU 437983A HU 197357 B HU197357 B HU 197357B
- Authority
- HU
- Hungary
- Prior art keywords
- protein
- solution
- denaturing
- refractive
- denaturing solution
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 354
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 347
- 238000000034 method Methods 0.000 title claims description 146
- 230000008569 process Effects 0.000 title claims description 69
- 238000004140 cleaning Methods 0.000 title description 3
- 239000000243 solution Substances 0.000 claims abstract description 214
- 239000000463 material Substances 0.000 claims abstract description 16
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 claims abstract description 14
- 238000000464 low-speed centrifugation Methods 0.000 claims abstract description 14
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 77
- 239000003795 chemical substances by application Substances 0.000 claims description 66
- 239000000872 buffer Substances 0.000 claims description 63
- 238000000746 purification Methods 0.000 claims description 43
- 239000004202 carbamide Substances 0.000 claims description 40
- 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 29
- 239000003638 chemical reducing agent Substances 0.000 claims description 27
- 239000007853 buffer solution Substances 0.000 claims description 23
- -1 sulfhydryl compound Chemical class 0.000 claims description 22
- 238000005119 centrifugation Methods 0.000 claims description 20
- ZRALSGWEFCBTJO-UHFFFAOYSA-N guanidine group Chemical group NC(=N)N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 claims description 19
- 239000003398 denaturant Substances 0.000 claims description 17
- 238000006243 chemical reaction Methods 0.000 claims description 14
- 108010024636 Glutathione Proteins 0.000 claims description 13
- 238000004113 cell culture Methods 0.000 claims description 13
- 239000000047 product Substances 0.000 claims description 13
- 230000002829 reductive effect Effects 0.000 claims description 13
- 239000007800 oxidant agent Substances 0.000 claims description 11
- 238000000703 high-speed centrifugation Methods 0.000 claims description 10
- 238000004519 manufacturing process Methods 0.000 claims description 9
- 230000001590 oxidative effect Effects 0.000 claims description 9
- 230000002147 killing effect Effects 0.000 claims description 8
- HAEPBEMBOAIUPN-UHFFFAOYSA-L sodium tetrathionate Chemical group O.O.[Na+].[Na+].[O-]S(=O)(=O)SSS([O-])(=O)=O HAEPBEMBOAIUPN-UHFFFAOYSA-L 0.000 claims description 8
- 238000011403 purification operation Methods 0.000 claims description 7
- 238000005063 solubilization Methods 0.000 claims description 6
- 230000007928 solubilization Effects 0.000 claims description 6
- LSNNMFCWUKXFEE-UHFFFAOYSA-N Sulfurous acid Chemical compound OS(O)=O LSNNMFCWUKXFEE-UHFFFAOYSA-N 0.000 claims description 5
- 239000002253 acid Substances 0.000 claims description 5
- 230000001413 cellular effect Effects 0.000 claims description 5
- 150000002357 guanidines Chemical class 0.000 claims description 5
- 238000004255 ion exchange chromatography Methods 0.000 claims description 5
- 238000007254 oxidation reaction Methods 0.000 claims description 5
- 239000002244 precipitate Substances 0.000 claims description 5
- 239000012460 protein solution Substances 0.000 claims description 3
- 238000010438 heat treatment Methods 0.000 claims description 2
- 239000003495 polar organic solvent Substances 0.000 claims description 2
- 206010029897 Obsessive thoughts Diseases 0.000 claims 2
- 238000010504 bond cleavage reaction Methods 0.000 claims 2
- 150000002019 disulfides Chemical class 0.000 claims 2
- 230000003213 activating effect Effects 0.000 claims 1
- 230000022534 cell killing Effects 0.000 claims 1
- 239000008366 buffered solution Substances 0.000 abstract description 2
- 235000018102 proteins Nutrition 0.000 description 313
- 210000004027 cell Anatomy 0.000 description 180
- 239000008188 pellet Substances 0.000 description 44
- 239000000725 suspension Substances 0.000 description 38
- 239000006228 supernatant Substances 0.000 description 34
- 239000002245 particle Substances 0.000 description 32
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 31
- 235000019333 sodium laurylsulphate Nutrition 0.000 description 31
- 108010000521 Human Growth Hormone Proteins 0.000 description 30
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 30
- 102000002265 Human Growth Hormone Human genes 0.000 description 29
- 239000002609 medium Substances 0.000 description 29
- 239000000854 Human Growth Hormone Substances 0.000 description 28
- YXFVVABEGXRONW-UHFFFAOYSA-N Toluene Chemical compound CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 27
- 238000000502 dialysis Methods 0.000 description 26
- 239000012530 fluid Substances 0.000 description 21
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 21
- 241000700605 Viruses Species 0.000 description 20
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 18
- 239000000122 growth hormone Substances 0.000 description 18
- 229960000789 guanidine hydrochloride Drugs 0.000 description 18
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 18
- 230000000694 effects Effects 0.000 description 17
- 239000013049 sediment Substances 0.000 description 17
- 239000000499 gel Substances 0.000 description 16
- 239000007788 liquid Substances 0.000 description 16
- 102000018997 Growth Hormone Human genes 0.000 description 15
- 108010051696 Growth Hormone Proteins 0.000 description 15
- 239000000203 mixture Substances 0.000 description 15
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 15
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 14
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 14
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 14
- 238000005342 ion exchange Methods 0.000 description 14
- 241000588724 Escherichia coli Species 0.000 description 13
- 229960005356 urokinase Drugs 0.000 description 13
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 12
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 12
- 230000004071 biological effect Effects 0.000 description 12
- 108090000467 Interferon-beta Proteins 0.000 description 10
- 239000012895 dilution Substances 0.000 description 10
- 238000010790 dilution Methods 0.000 description 10
- 229960003180 glutathione Drugs 0.000 description 10
- 150000002500 ions Chemical class 0.000 description 10
- GEHJYWRUCIMESM-UHFFFAOYSA-L sodium sulfite Chemical compound [Na+].[Na+].[O-]S([O-])=O GEHJYWRUCIMESM-UHFFFAOYSA-L 0.000 description 10
- 239000002904 solvent Substances 0.000 description 10
- 125000003396 thiol group Chemical group [H]S* 0.000 description 10
- 108010053070 Glutathione Disulfide Proteins 0.000 description 9
- 102000003996 Interferon-beta Human genes 0.000 description 9
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 9
- 108010006025 bovine growth hormone Proteins 0.000 description 9
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 9
- 238000002523 gelfiltration Methods 0.000 description 9
- 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 description 9
- 229960004198 guanidine Drugs 0.000 description 9
- 239000012535 impurity Substances 0.000 description 9
- 241001646716 Escherichia coli K-12 Species 0.000 description 8
- 241000710198 Foot-and-mouth disease virus Species 0.000 description 8
- 108020004511 Recombinant DNA Proteins 0.000 description 8
- 102000036639 antigens Human genes 0.000 description 8
- 108091007433 antigens Proteins 0.000 description 8
- 238000004925 denaturation Methods 0.000 description 8
- 239000011347 resin Substances 0.000 description 8
- 229920005989 resin Polymers 0.000 description 8
- 150000003839 salts Chemical class 0.000 description 8
- 238000003556 assay Methods 0.000 description 7
- 239000000284 extract Substances 0.000 description 7
- 239000008187 granular material Substances 0.000 description 7
- 238000002955 isolation Methods 0.000 description 7
- 238000001556 precipitation Methods 0.000 description 7
- 108010064037 prorennin Proteins 0.000 description 7
- 239000011780 sodium chloride Substances 0.000 description 7
- 230000001133 acceleration Effects 0.000 description 6
- 239000000427 antigen Substances 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 6
- 238000004587 chromatography analysis Methods 0.000 description 6
- 239000000356 contaminant Substances 0.000 description 6
- 239000012634 fragment Substances 0.000 description 6
- 238000003018 immunoassay Methods 0.000 description 6
- 230000002285 radioactive effect Effects 0.000 description 6
- 239000006176 redox buffer Substances 0.000 description 6
- 230000000717 retained effect Effects 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
- 101710132601 Capsid protein Proteins 0.000 description 5
- 101710094648 Coat protein Proteins 0.000 description 5
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 5
- 108010074328 Interferon-gamma Proteins 0.000 description 5
- 102000008070 Interferon-gamma Human genes 0.000 description 5
- 101710125418 Major capsid protein Proteins 0.000 description 5
- 101710141454 Nucleoprotein Proteins 0.000 description 5
- 101710083689 Probable capsid protein Proteins 0.000 description 5
- 239000012506 Sephacryl® Substances 0.000 description 5
- 230000001580 bacterial effect Effects 0.000 description 5
- 238000004166 bioassay Methods 0.000 description 5
- 239000003153 chemical reaction reagent Substances 0.000 description 5
- 238000012258 culturing Methods 0.000 description 5
- 230000036425 denaturation Effects 0.000 description 5
- 239000003599 detergent Substances 0.000 description 5
- 238000004090 dissolution Methods 0.000 description 5
- 230000005484 gravity Effects 0.000 description 5
- 239000002808 molecular sieve Substances 0.000 description 5
- 238000001742 protein purification Methods 0.000 description 5
- 230000007420 reactivation Effects 0.000 description 5
- 238000011084 recovery Methods 0.000 description 5
- URGAHOPLAPQHLN-UHFFFAOYSA-N sodium aluminosilicate Chemical compound [Na+].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O URGAHOPLAPQHLN-UHFFFAOYSA-N 0.000 description 5
- 235000010265 sodium sulphite Nutrition 0.000 description 5
- 238000002604 ultrasonography Methods 0.000 description 5
- 241000894006 Bacteria Species 0.000 description 4
- GUBGYTABKSRVRQ-WFVLMXAXSA-N DEAE-cellulose Chemical compound OC1C(O)C(O)C(CO)O[C@H]1O[C@@H]1C(CO)OC(O)C(O)C1O GUBGYTABKSRVRQ-WFVLMXAXSA-N 0.000 description 4
- 101000599940 Homo sapiens Interferon gamma Proteins 0.000 description 4
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 4
- 206010037742 Rabies Diseases 0.000 description 4
- 239000007983 Tris buffer Substances 0.000 description 4
- 239000007864 aqueous solution Substances 0.000 description 4
- 239000001913 cellulose Substances 0.000 description 4
- 229920002678 cellulose Polymers 0.000 description 4
- 239000002738 chelating agent Substances 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 238000000326 densiometry Methods 0.000 description 4
- 239000006185 dispersion Substances 0.000 description 4
- 238000000605 extraction Methods 0.000 description 4
- 238000005227 gel permeation chromatography Methods 0.000 description 4
- 238000001727 in vivo Methods 0.000 description 4
- 239000013612 plasmid Substances 0.000 description 4
- 239000000523 sample Substances 0.000 description 4
- 239000002002 slurry Substances 0.000 description 4
- 230000003381 solubilizing effect Effects 0.000 description 4
- NSHWGYPCYVZQOD-UHFFFAOYSA-N 2-(1h-indol-2-yl)prop-2-enoic acid Chemical compound C1=CC=C2NC(C(=C)C(=O)O)=CC2=C1 NSHWGYPCYVZQOD-UHFFFAOYSA-N 0.000 description 3
- 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 3
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 3
- GOLXRNDWAUTYKT-UHFFFAOYSA-N 3-(1H-indol-3-yl)propanoic acid Chemical compound C1=CC=C2C(CCC(=O)O)=CNC2=C1 GOLXRNDWAUTYKT-UHFFFAOYSA-N 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
- 238000012270 DNA recombination Methods 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 3
- 102000014150 Interferons Human genes 0.000 description 3
- 108010050904 Interferons Proteins 0.000 description 3
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 3
- 229910019142 PO4 Inorganic materials 0.000 description 3
- 108010001014 Plasminogen Activators Proteins 0.000 description 3
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 description 3
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 239000006285 cell suspension Substances 0.000 description 3
- 210000002421 cell wall Anatomy 0.000 description 3
- 230000003196 chaotropic effect Effects 0.000 description 3
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 3
- 235000018417 cysteine Nutrition 0.000 description 3
- 210000000805 cytoplasm Anatomy 0.000 description 3
- 238000010586 diagram Methods 0.000 description 3
- 230000029087 digestion Effects 0.000 description 3
- 239000002270 dispersing agent Substances 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 238000001914 filtration Methods 0.000 description 3
- 239000008103 glucose Substances 0.000 description 3
- 230000012010 growth Effects 0.000 description 3
- 239000003456 ion exchange resin Substances 0.000 description 3
- 229920003303 ion-exchange polymer Polymers 0.000 description 3
- 238000001000 micrograph Methods 0.000 description 3
- 230000007935 neutral effect Effects 0.000 description 3
- 230000003287 optical effect Effects 0.000 description 3
- 230000003647 oxidation Effects 0.000 description 3
- 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 description 3
- 230000036961 partial effect Effects 0.000 description 3
- 238000002135 phase contrast microscopy Methods 0.000 description 3
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 3
- 239000010452 phosphate Substances 0.000 description 3
- 239000008363 phosphate buffer Substances 0.000 description 3
- 230000003389 potentiating effect Effects 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 108090000765 processed proteins & peptides Proteins 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- VGTPCRGMBIAPIM-UHFFFAOYSA-M sodium thiocyanate Chemical compound [Na+].[S-]C#N VGTPCRGMBIAPIM-UHFFFAOYSA-M 0.000 description 3
- 238000000527 sonication Methods 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 229960000187 tissue plasminogen activator Drugs 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 2
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-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
- 241001465754 Metazoa Species 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- PXHVJJICTQNCMI-UHFFFAOYSA-N Nickel Chemical compound [Ni] PXHVJJICTQNCMI-UHFFFAOYSA-N 0.000 description 2
- 102000001938 Plasminogen Activators Human genes 0.000 description 2
- 206010039491 Sarcoma Diseases 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 150000001413 amino acids Chemical group 0.000 description 2
- 238000009835 boiling Methods 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 210000000170 cell membrane Anatomy 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 238000001816 cooling Methods 0.000 description 2
- UFULAYFCSOUIOV-UHFFFAOYSA-N cysteamine Chemical compound NCCS UFULAYFCSOUIOV-UHFFFAOYSA-N 0.000 description 2
- 229960002433 cysteine Drugs 0.000 description 2
- 238000011026 diafiltration Methods 0.000 description 2
- 238000007865 diluting Methods 0.000 description 2
- 125000002228 disulfide group Chemical group 0.000 description 2
- 238000011067 equilibration Methods 0.000 description 2
- 230000002349 favourable effect Effects 0.000 description 2
- 238000001502 gel electrophoresis Methods 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 238000000265 homogenisation Methods 0.000 description 2
- 125000004029 hydroxymethyl group Chemical group [H]OC([H])([H])* 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 229940047124 interferons Drugs 0.000 description 2
- 239000000543 intermediate Substances 0.000 description 2
- 230000002427 irreversible effect Effects 0.000 description 2
- 229920002521 macromolecule Polymers 0.000 description 2
- 229960003151 mercaptamine Drugs 0.000 description 2
- VNWKTOKETHGBQD-UHFFFAOYSA-N methane Chemical compound C VNWKTOKETHGBQD-UHFFFAOYSA-N 0.000 description 2
- 230000000269 nucleophilic effect Effects 0.000 description 2
- 230000004962 physiological condition Effects 0.000 description 2
- 229940127126 plasminogen activator Drugs 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 239000011148 porous material Substances 0.000 description 2
- 230000006920 protein precipitation Effects 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 239000010421 standard material Substances 0.000 description 2
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 2
- 238000006277 sulfonation reaction Methods 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 238000009210 therapy by ultrasound Methods 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 2
- 238000011179 visual inspection Methods 0.000 description 2
- 239000011800 void material Substances 0.000 description 2
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 1
- WZIMSXIXZTUBSO-UHFFFAOYSA-N 2-[[bis(carboxymethyl)amino]methyl-(carboxymethyl)amino]acetic acid Chemical compound OC(=O)CN(CC(O)=O)CN(CC(O)=O)CC(O)=O WZIMSXIXZTUBSO-UHFFFAOYSA-N 0.000 description 1
- TVZXDXULHJPKPB-UHFFFAOYSA-N 3-(aminomethyl)-3-(2-hydroxyethyl)pentane-1,5-diol Chemical compound OCCC(CN)(CCO)CCO TVZXDXULHJPKPB-UHFFFAOYSA-N 0.000 description 1
- VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 0.000 description 1
- 101000914103 Bos taurus Chymosin Proteins 0.000 description 1
- JJDDPDHSLLONIF-UHFFFAOYSA-N C=C.CC(O)=O.CC(O)=O.CC(O)=O.CC(O)=O Chemical compound C=C.CC(O)=O.CC(O)=O.CC(O)=O.CC(O)=O JJDDPDHSLLONIF-UHFFFAOYSA-N 0.000 description 1
- 108090000565 Capsid Proteins Proteins 0.000 description 1
- 241000700198 Cavia Species 0.000 description 1
- 108090000746 Chymosin Proteins 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 1
- 208000007212 Foot-and-Mouth Disease Diseases 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 241000700721 Hepatitis B virus Species 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 102000006992 Interferon-alpha Human genes 0.000 description 1
- 108010047761 Interferon-alpha Proteins 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N L-cystine Chemical compound [O-]C(=O)[C@@H]([NH3+])CSSC[C@H]([NH3+])C([O-])=O LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- BAVYZALUXZFZLV-UHFFFAOYSA-N Methylamine Chemical compound NC BAVYZALUXZFZLV-UHFFFAOYSA-N 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- NVULURMXLCMOCB-UHFFFAOYSA-N OCC(C(N)N)(CO)CO Chemical compound OCC(C(N)N)(CO)CO NVULURMXLCMOCB-UHFFFAOYSA-N 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 241000282898 Sus scrofa Species 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108010027252 Trypsinogen Proteins 0.000 description 1
- 102000018690 Trypsinogen Human genes 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 239000003463 adsorbent Substances 0.000 description 1
- 238000005273 aeration Methods 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 239000000908 ammonium hydroxide Substances 0.000 description 1
- 238000005349 anion exchange Methods 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 239000012062 aqueous buffer Substances 0.000 description 1
- 239000012736 aqueous medium Substances 0.000 description 1
- 239000012298 atmosphere Substances 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 239000012148 binding buffer Substances 0.000 description 1
- 210000000601 blood cell Anatomy 0.000 description 1
- 230000003139 buffering effect Effects 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 238000005341 cation exchange Methods 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 238000011210 chromatographic step Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000007820 coagulation assay Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 238000004891 communication Methods 0.000 description 1
- 229960003067 cystine Drugs 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 239000013578 denaturing buffer Substances 0.000 description 1
- 238000010217 densitometric analysis Methods 0.000 description 1
- 238000010612 desalination reaction Methods 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 229910001882 dioxygen Inorganic materials 0.000 description 1
- 230000006334 disulfide bridging Effects 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
- MOTZDAYCYVMXPC-UHFFFAOYSA-N dodecyl hydrogen sulfate Chemical compound CCCCCCCCCCCCOS(O)(=O)=O MOTZDAYCYVMXPC-UHFFFAOYSA-N 0.000 description 1
- 229940043264 dodecyl sulfate Drugs 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000007824 enzymatic assay Methods 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 238000001952 enzyme assay Methods 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 239000012520 frozen sample Substances 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 230000003054 hormonal effect Effects 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 230000036571 hydration Effects 0.000 description 1
- 238000006703 hydration reaction Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 230000001665 lethal effect Effects 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 238000010297 mechanical methods and process Methods 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- IZXGZAJMDLJLMF-UHFFFAOYSA-N methylaminomethanol Chemical compound CNCO IZXGZAJMDLJLMF-UHFFFAOYSA-N 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 229910000403 monosodium phosphate Inorganic materials 0.000 description 1
- 235000019799 monosodium phosphate Nutrition 0.000 description 1
- 229910052759 nickel Inorganic materials 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 239000012454 non-polar solvent Substances 0.000 description 1
- 231100001160 nonlethal Toxicity 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 229920000058 polyacrylate Polymers 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 210000004777 protein coat Anatomy 0.000 description 1
- 230000007065 protein hydrolysis Effects 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 238000010992 reflux Methods 0.000 description 1
- 238000004153 renaturation Methods 0.000 description 1
- 238000001226 reprecipitation Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000009751 slip forming Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- AJPJDKMHJJGVTQ-UHFFFAOYSA-M sodium dihydrogen phosphate Chemical compound [Na+].OP(O)([O-])=O AJPJDKMHJJGVTQ-UHFFFAOYSA-M 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 239000011550 stock solution Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 125000001273 sulfonato group Chemical group [O-]S(*)(=O)=O 0.000 description 1
- 125000004434 sulfur atom Chemical group 0.000 description 1
- 150000003567 thiocyanates Chemical class 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- GKODZWOPPOTFGA-UHFFFAOYSA-N tris(hydroxyethyl)aminomethane Chemical compound OCCC(N)(CCO)CCO GKODZWOPPOTFGA-UHFFFAOYSA-N 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 230000009385 viral infection Effects 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6478—Aspartic endopeptidases (3.4.23)
- C12N9/6481—Pepsins (3.4.23.1; 3.4.23.2; 3.4.23.3)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
- C07K1/1133—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure by redox-reactions involving cystein/cystin side chains
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6456—Plasminogen activators
- C12N9/6462—Plasminogen activators u-Plasminogen activator (3.4.21.73), i.e. urokinase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
- C12Y304/21073—Serine endopeptidases (3.4.21) u-Plasminogen activator (3.4.21.73), i.e. urokinase
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Analytical Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Enzymes And Modification Thereof (AREA)
Applications Claiming Priority (8)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US45235682A | 1982-12-22 | 1982-12-22 | |
| US45234482A | 1982-12-22 | 1982-12-22 | |
| US45235782A | 1982-12-22 | 1982-12-22 | |
| US45225282A | 1982-12-22 | 1982-12-22 | |
| US45218782A | 1982-12-22 | 1982-12-22 | |
| US45236382A | 1982-12-22 | 1982-12-22 | |
| US45225382A | 1982-12-22 | 1982-12-22 | |
| US45235582A | 1982-12-22 | 1982-12-22 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| HU197357B true HU197357B (en) | 1989-03-28 |
Family
ID=27575443
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| HU834379A HU197357B (en) | 1982-12-22 | 1983-12-21 | Process for cleaning and reactivating precipitated heterologous proteins |
Country Status (12)
| Country | Link |
|---|---|
| EP (1) | EP0114506B1 (en, 2012) |
| JP (1) | JP2575604B2 (en, 2012) |
| AU (1) | AU568109B2 (en, 2012) |
| BR (1) | BR8307086A (en, 2012) |
| CA (1) | CA1219234A (en, 2012) |
| DE (1) | DE3380850D1 (en, 2012) |
| GR (1) | GR79124B (en, 2012) |
| HU (1) | HU197357B (en, 2012) |
| IL (1) | IL70474A (en, 2012) |
| MX (1) | MX166885B (en, 2012) |
| NZ (1) | NZ206615A (en, 2012) |
| PT (1) | PT77866B (en, 2012) |
Families Citing this family (87)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4342832A (en) * | 1979-07-05 | 1982-08-03 | Genentech, Inc. | Method of constructing a replicable cloning vehicle having quasi-synthetic genes |
| US4476049A (en) * | 1983-09-20 | 1984-10-09 | Hoffmann-La Roche Inc. | Method for the extraction of immune interferon |
| JPH064680B2 (ja) * | 1985-01-09 | 1994-01-19 | 武田薬品工業株式会社 | 高濃度ヒトγ型インターフェロンフラグメント水溶液の製造法 |
| JPS60155137A (ja) * | 1984-01-23 | 1985-08-15 | Takeda Chem Ind Ltd | 高濃度ヒトγ型インタ−フエロン水溶液の製造法 |
| US4530787A (en) * | 1984-03-28 | 1985-07-23 | Cetus Corporation | Controlled oxidation of microbially produced cysteine-containing proteins |
| JPS60258129A (ja) * | 1984-06-05 | 1985-12-20 | Kyowa Hakko Kogyo Co Ltd | インタ−フエロンの活性化法 |
| ATE64956T1 (de) * | 1984-06-14 | 1991-07-15 | Ciba Geigy Ag | Verfahren zur herstellung von thrombininhibitoren. |
| CA1267615A (en) * | 1984-08-27 | 1990-04-10 | Dan Hadary | Method for recovering purified growth hormones from genetically engineered microorganisms |
| US5871956A (en) * | 1984-12-06 | 1999-02-16 | Amgen Inc. | Recombinant methods for production of serine inhibitors and DNA sequences useful for same |
| US6291662B1 (en) | 1984-12-05 | 2001-09-18 | Amgen Inc. | Recombinant methods for production of serine protease inhibitors and DNA sequences |
| US6132990A (en) * | 1984-12-06 | 2000-10-17 | Amgen Boulder Inc. | Recombinant methods for production of serine protease inhibitors and DNA sequences useful for same |
| IL95223A (en) * | 1984-12-06 | 1992-08-18 | Synergen Biolog Inc | Dna sequence for production of serine protease inhibitors |
| US5900400A (en) * | 1984-12-06 | 1999-05-04 | Amgen Inc. | Serine protease inhibitor analogs |
| WO1986004608A1 (en) * | 1985-02-05 | 1986-08-14 | Synergen Biologicals, Inc. | Metalloproteinase inhibitor sequence recombinant vector system for using same and recombinant-dna method for the manufacture of same |
| US4731440A (en) * | 1985-02-22 | 1988-03-15 | Monsanto Company | Method of somatotropin solubilization using dimethylsulfone and naturation |
| US4861868A (en) | 1985-02-22 | 1989-08-29 | Monsanto Company | Production of proteins in procaryotes |
| ES8800957A1 (es) * | 1985-02-22 | 1987-12-01 | Monsanto Co | Un metodo para la solubilizacion y renaturalizacion de proteina somatotropina |
| US4652630A (en) * | 1985-02-22 | 1987-03-24 | Monsanto Company | Method of somatotropin naturation |
| US6084073A (en) * | 1985-03-25 | 2000-07-04 | Chiron Corporation | Recombinant ricin toxin |
| FR2579223B1 (fr) * | 1985-03-25 | 1988-12-09 | Genetica | Procede de preparation microbiologique de la serum-albumine humaine |
| DE3511011A1 (de) * | 1985-03-27 | 1986-10-02 | Hoechst Ag, 6230 Frankfurt | Verfahren zur isolierung und reinigung von (alpha)-interferonen |
| GB8508340D0 (en) * | 1985-03-29 | 1985-05-09 | Creighton T E | Production of protein |
| DE3683186D1 (de) | 1985-04-25 | 1992-02-13 | Hoffmann La Roche | Rekombinantes humaninterleukin-1. |
| JPH0640832B2 (ja) * | 1985-05-10 | 1994-06-01 | 味の素株式会社 | インタ−ロイキン２ポリペプチドの回収方法 |
| EP0226639B1 (en) * | 1985-05-29 | 1990-11-14 | The Green Cross Corporation | Process for preparing heterogenic protein |
| US5248769A (en) * | 1985-06-26 | 1993-09-28 | Cetus Oncology Corporation | Process for recovering refractile bodies containing heterologous proteins from microbial hosts |
| EP0229110B1 (en) | 1985-06-26 | 1992-05-20 | The Upjohn Company | Solubilization and oxidation of somatotropin from transformed microorganisms |
| US4748234A (en) * | 1985-06-26 | 1988-05-31 | Cetus Corporation | Process for recovering refractile bodies containing heterologous proteins from microbial hosts |
| US4766224A (en) * | 1985-08-19 | 1988-08-23 | International Minerals & Chemical Corp. | Purification and activation of proteins from insoluble inclusion bodies |
| US4656255A (en) * | 1985-09-09 | 1987-04-07 | International Minerals & Chemical Corp. | Protein recovery |
| DE3537708A1 (de) * | 1985-10-23 | 1987-04-23 | Boehringer Mannheim Gmbh | Verfahren zur aktivierung von t-pa nach expression in prokaryonten |
| US5453363A (en) * | 1985-10-23 | 1995-09-26 | Boehringer Mannheim Gmbh | Process for the activation of t-PA or Ing after genetic expression in prokaryotes |
| US4766205A (en) * | 1985-11-13 | 1988-08-23 | Beatrice Companies, Inc. | Method for isolation of recombinant polypeptides in biologically active forms |
| US4734362A (en) * | 1986-02-03 | 1988-03-29 | Cambridge Bioscience Corporation | Process for purifying recombinant proteins, and products thereof |
| US5831022A (en) * | 1986-02-18 | 1998-11-03 | Hoffmann-La Roche Inc. | Purification of recombinant human IL-1α |
| FR2594846B1 (fr) * | 1986-02-21 | 1989-10-20 | Genetica | Procede de preparation de la serum albumine humaine mature |
| US4689401A (en) * | 1986-03-06 | 1987-08-25 | Cetus Corporation | Method of recovering microbially produced recombinant ricin toxin a chain |
| DE3611817A1 (de) * | 1986-04-08 | 1987-10-15 | Boehringer Mannheim Gmbh | Verfahren zur renaturierung von proteinen |
| US4705848A (en) * | 1986-06-02 | 1987-11-10 | International Minerals & Chemical Corp. | Isolation of bioactive, monomeric growth hormone |
| DE3618817A1 (de) * | 1986-06-04 | 1987-12-10 | Behringwerke Ag | Verfahren zur gewinnung aktiver proteine aus einer biologisch inaktiven form |
| US4801686A (en) * | 1986-09-04 | 1989-01-31 | Immunex Corporation | Purification of recombinant interleukin-1 |
| US5179199A (en) * | 1986-10-20 | 1993-01-12 | Genzyme Corporation | Protein purification |
| AU612133B2 (en) * | 1987-02-20 | 1991-07-04 | Natinco Nv | Production of proteins in active forms |
| US5026828A (en) * | 1987-02-27 | 1991-06-25 | Merck & Co., Inc. | Method of purifying recombinant pres-1/S-2/S/S hepatitis B antigen from yeast |
| IL86090A (en) * | 1987-04-16 | 1993-03-15 | Cetus Oncology Corp | 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 |
| CA1339757C (en) | 1987-04-16 | 1998-03-17 | Robert F. Halenbeck | Production of purified biologically active, bacterially produced recombinant human csf-1 |
| WO1988008428A1 (en) * | 1987-04-28 | 1988-11-03 | Amgen Inc. | Method for purifying granulocyte/macrophage colony stimulating factor |
| US5162507A (en) * | 1987-05-11 | 1992-11-10 | Cetus Corporation | Process for recovering purified, oxidized, renatured recombinant interleukin-2 from microorganisms |
| WO1988008849A1 (en) * | 1987-05-11 | 1988-11-17 | Cetus Corporation | Process for recovering purified, oxidized, renatured recombinant interleukin-2 from microorganisms |
| US4931543A (en) * | 1987-05-11 | 1990-06-05 | Cetus Corporation | Process for recovering microbially produced interleukin-2 |
| JP2669859B2 (ja) * | 1987-08-04 | 1997-10-29 | 協和醗酵工業株式会社 | タンパク質の再活性化法 |
| US4985544A (en) * | 1987-08-04 | 1991-01-15 | Kyowa Hakko Kogyo Co., Ltd. | Process for renaturing fish growth hormone |
| US5011915A (en) * | 1987-10-26 | 1991-04-30 | Merck & Co., Inc. | Process for purifying recombinant hepatitis antigens |
| EP0325691B1 (de) * | 1988-01-25 | 1993-04-07 | Consortium für elektrochemische Industrie GmbH | Verfahren zur Solubilisierung von unlöslichem Protein |
| JPH01257491A (ja) * | 1988-04-08 | 1989-10-13 | Tosoh Corp | 不溶性融合異種蛋白質の処理方法 |
| US4999422A (en) * | 1988-04-15 | 1991-03-12 | Biogen, N.V. | Continuous method of refolding proteins |
| JP2812760B2 (ja) * | 1988-05-31 | 1998-10-22 | カイロン コーポレイション | 微生物宿主から異種蛋白質を含有する屈折体を回収する方法 |
| US5089473A (en) | 1988-08-29 | 1992-02-18 | Monsanto Company | Somatotropin variants and their use |
| CA1340586C (en) * | 1988-09-23 | 1999-06-08 | Cetus Corporation | Process for recovering microbially produced interferon-beta |
| DE3832898A1 (de) * | 1988-09-28 | 1990-04-12 | Boehringer Mannheim Gmbh | Praeparat von in prokaryonten exprimiertem plasminogenaktivator |
| DE3835350A1 (de) * | 1988-10-17 | 1990-04-19 | Boehringer Mannheim Gmbh | Aktivierung von gentechnologisch hergestellten, in prokaryonten exprimierten antikoerpern |
| US5179196A (en) * | 1989-05-04 | 1993-01-12 | Sri International | Purification of proteins employing ctap-iii fusions |
| GB8927546D0 (en) * | 1989-12-06 | 1990-02-07 | Ciba Geigy | Process for the production of biologically active tgf-beta |
| DE4039415A1 (de) | 1990-02-03 | 1991-08-08 | Boehringer Mannheim Gmbh | Verfahren zur herstellung rekombinanter proteine ohne n-terminalen methioninrest |
| US5023323A (en) * | 1990-09-12 | 1991-06-11 | Monsanto Company | Method of somatotropin naturation |
| JPH04113933U (ja) * | 1991-03-22 | 1992-10-06 | 富泰 本多 | 化粧板 |
| JPH084290Y2 (ja) * | 1991-03-22 | 1996-02-07 | 富泰 本多 | 化粧板 |
| US6869925B1 (en) * | 1992-09-09 | 2005-03-22 | Amgen Inc. | Inhibition of retrovirus infection |
| US5399677A (en) * | 1993-12-07 | 1995-03-21 | Genetics Institute, Inc. | Mutants of bone morphogenetic proteins |
| US6017880A (en) * | 1994-03-09 | 2000-01-25 | Amgen Inc. | Inhibition of retrovirus infection |
| US5437986A (en) * | 1994-06-22 | 1995-08-01 | Schering Corporation | Extraction of heterologous insoluble proteins from bacteria |
| FI970230L (fi) * | 1994-07-25 | 1997-01-20 | Ciba Geigy Ag | Menetelmä proteiinien, kuten yhdistelmä-DNA-hirudiinin tai -epidermaalisen kasvutekijän laskostamiseksi |
| TW517059B (en) | 1994-07-25 | 2003-01-11 | Ciba Geigy Ag | New process for the production of biologically active protein |
| US6037145A (en) * | 1994-09-07 | 2000-03-14 | Suntory Limited | Process for production of protein |
| GB9425138D0 (en) | 1994-12-12 | 1995-02-08 | Dynal As | Isolation of nucleic acid |
| EP0904355B1 (de) * | 1996-06-11 | 2004-03-03 | Boehringer Mannheim Gmbh | Verfahren zur aktivierung von denaturiertem protein |
| US5914390A (en) * | 1997-05-12 | 1999-06-22 | Celtrix Pharmaceuticals, Inc. | Methods for increasing yields of recombinant proteins |
| WO1999010483A2 (de) * | 1997-08-22 | 1999-03-04 | Roche Diagnostics Gmbh | Autokatalytisch aktivierbare vorstufen von proteasen und deren verwendung |
| JP3734634B2 (ja) | 1999-03-03 | 2006-01-11 | ヒゲタ醤油株式会社 | タンパク質の活性化方法及び該装置 |
| IN187900B (en, 2012) * | 2000-02-01 | 2002-07-20 | Torrent Pharmaceuticals Ltd | |
| KR100409092B1 (ko) * | 2000-12-22 | 2003-12-11 | 주)녹십자 | 단백질의 제조 방법 |
| KR101099398B1 (ko) | 2003-09-30 | 2011-12-27 | 아스비오파마 가부시키가이샤 | ＯｍｐＴ 프로테아제 변이체를 이용한 폴리펩티드의 절단 방법 |
| EP1910415A4 (en) * | 2005-07-25 | 2010-08-11 | Trubion Pharmaceuticals Inc | COMPOSITIONS AND PROCESSES FOR PROTEIN DEGREGATION |
| EP2547699B1 (en) | 2010-03-17 | 2016-10-19 | ratiopharm GmbH | Method for obtaining biologically active recombinant human g-csf |
| JP5805943B2 (ja) * | 2010-12-08 | 2015-11-10 | 株式会社北里大塚バイオメディカルアッセイ研究所 | 百日咳菌のＦｉｍ３の製造方法、及び、百日咳の検出方法 |
| USD1086051S1 (en) * | 2022-09-30 | 2025-07-29 | Maxcyte, Inc. | Electroporation gasket |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4350764A (en) * | 1980-03-10 | 1982-09-21 | The Regents Of The University Of California | Microbiological synthesis of beta endorphin |
| AU564690B2 (en) * | 1980-04-03 | 1987-08-20 | Biogen Idec Ma Inc. | Process for producing human fibroblast interferon-like polypeptides using recombinant dna |
| IL63916A0 (en) * | 1980-09-25 | 1981-12-31 | Genentech Inc | Microbial production of human fibroblast interferon |
| AU561343B2 (en) * | 1981-10-19 | 1987-05-07 | Genentech Inc. | Human immune interferon by recombinant dna |
| JPS58157800A (ja) * | 1982-03-16 | 1983-09-19 | Sankyo Co Ltd | プラスミドｐｓａｎ１８１ |
-
1983
- 1983-12-16 GR GR73270A patent/GR79124B/el unknown
- 1983-12-18 IL IL70474A patent/IL70474A/xx not_active IP Right Cessation
- 1983-12-19 NZ NZ206615A patent/NZ206615A/en unknown
- 1983-12-20 AU AU22594/83A patent/AU568109B2/en not_active Expired
- 1983-12-21 HU HU834379A patent/HU197357B/hu unknown
- 1983-12-21 JP JP58241820A patent/JP2575604B2/ja not_active Expired - Lifetime
- 1983-12-21 EP EP83307840A patent/EP0114506B1/en not_active Expired
- 1983-12-21 CA CA000443903A patent/CA1219234A/en not_active Expired
- 1983-12-21 MX MX199852A patent/MX166885B/es unknown
- 1983-12-21 PT PT77866A patent/PT77866B/pt unknown
- 1983-12-21 DE DE8383307840T patent/DE3380850D1/de not_active Expired
- 1983-12-22 BR BR8307086A patent/BR8307086A/pt unknown
Also Published As
| Publication number | Publication date |
|---|---|
| IL70474A0 (en) | 1984-03-30 |
| NZ206615A (en) | 1988-03-30 |
| PT77866B (en) | 1986-04-09 |
| MX166885B (es) | 1993-02-10 |
| CA1219234A (en) | 1987-03-17 |
| EP0114506B1 (en) | 1989-11-15 |
| BR8307086A (pt) | 1985-02-12 |
| AU2259483A (en) | 1984-06-28 |
| GR79124B (en, 2012) | 1984-10-02 |
| AU568109B2 (en) | 1987-12-17 |
| EP0114506A1 (en) | 1984-08-01 |
| JP2575604B2 (ja) | 1997-01-29 |
| JPS59161321A (ja) | 1984-09-12 |
| DE3380850D1 (en) | 1989-12-21 |
| IL70474A (en) | 1989-09-28 |
| PT77866A (en) | 1984-01-01 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| HU197357B (en) | Process for cleaning and reactivating precipitated heterologous proteins | |
| US4512922A (en) | Purification and activity assurance of precipitated heterologous proteins | |
| US4620948A (en) | Purification and activity assurance of precipitated heterologous proteins | |
| US4511502A (en) | Purification and activity assurance of precipitated heterologous proteins | |
| US4518526A (en) | Purification and activity assurance of precipitated heterologous proteins | |
| US4599197A (en) | Purification and activity assurance of precipitated heterologous proteins | |
| US4511503A (en) | Purification and activity assurance of precipitated heterologous proteins | |
| US6471500B1 (en) | Process for producing erythropoietin containing no animal proteins | |
| JP2608081B2 (ja) | 組換えタンパク質の精製方法及びその製品 | |
| US4766224A (en) | Purification and activation of proteins from insoluble inclusion bodies | |
| NO863424L (no) | Fremgangsmaate for rensing av et interferon. | |
| AU593548B2 (en) | A process for the production of a protein | |
| EP0215625B1 (en) | Protein recovery | |
| JPH06102034B2 (ja) | タンパク質の生産方法 | |
| NO300067B1 (no) | Fremgangsmåte for å tilveiebringe renset, biologisk aktiv CSF-1 dimer | |
| EP0173215B1 (en) | Method for recovering purified growth hormones from genetically engineered microorganisms | |
| US5340926A (en) | Process for the recovery of recombinantly produced protein from insoluble aggregate | |
| KR960003548B1 (ko) | 생물활성을 갖는 모노머성 성장호르몬의 분리방법 | |
| JPH01257491A (ja) | 不溶性融合異種蛋白質の処理方法 | |
| JP2517100B2 (ja) | 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 | |
| US4436816A (en) | Cell growth promoting material | |
| IE56376B1 (en) | Methods of purification and reactivation of precipitated heterologous proteins | |
| EP0578472A2 (en) | A process for recovering peptides expressed as fusion proteins | |
| WO2004050672A2 (en) | Process for the extraction and isolation of insulin from recombinant sources | |
| JP3040189B2 (ja) | タンパクの抽出方法 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| HU90 | Patent valid on 900628 |