UA62925C2 - METHOD FOR PRODUCTION OF rDSPA a1 - Google Patents

METHOD FOR PRODUCTION OF rDSPA a1 Download PDF

Info

Publication number: UA62925C2
Authority: UA; Ukraine
Prior art keywords: resin; fact; protein; stage; buffer
Prior art date: 1996-02-05

Application number

UA98094695A

Other languages

English (en)

Ukrainian (uk)

Original Assignee

Schering Ag

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1996-02-05

Filing date

1997-01-31

Publication date

2004-01-15

1997-01-31 Application filed by Schering Ag filed Critical Schering Ag

2004-01-15 Publication of UA62925C2 publication Critical patent/UA62925C2/uk

Links

238000004519 manufacturing process Methods 0.000 title abstract description 6
238000001042 affinity chromatography Methods 0.000 claims abstract description 22
239000000872 buffer Substances 0.000 claims description 80
239000011347 resin Substances 0.000 claims description 79
229920005989 resin Polymers 0.000 claims description 79
102000004169 proteins and genes Human genes 0.000 claims description 56
108090000623 proteins and genes Proteins 0.000 claims description 56
238000000034 method Methods 0.000 claims description 42
230000004927 fusion Effects 0.000 claims description 27
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 26
239000011159 matrix material Substances 0.000 claims description 26
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 claims description 24
239000003729 cation exchange resin Substances 0.000 claims description 24
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 20
238000005406 washing Methods 0.000 claims description 19
239000012535 impurity Substances 0.000 claims description 18
238000000746 purification Methods 0.000 claims description 18
239000008187 granular material Substances 0.000 claims description 17
239000002904 solvent Substances 0.000 claims description 16
LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical group OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 claims description 15
238000011068 loading method Methods 0.000 claims description 12
241001459693 Dipterocarpus zeylanicus Species 0.000 claims description 11
VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 claims description 11
239000002245 particle Substances 0.000 claims description 11
239000000741 silica gel Substances 0.000 claims description 11
229910002027 silica gel Inorganic materials 0.000 claims description 11
239000004471 Glycine Substances 0.000 claims description 10
125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims description 10
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 9
229920000642 polymer Polymers 0.000 claims description 9
239000000356 contaminant Substances 0.000 claims description 8
239000001488 sodium phosphate Substances 0.000 claims description 8
229910000162 sodium phosphate Inorganic materials 0.000 claims description 8
RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 claims description 8
229920002873 Polyethylenimine Polymers 0.000 claims description 7
BLRPTPMANUNPDV-UHFFFAOYSA-N Silane Chemical compound [SiH4] BLRPTPMANUNPDV-UHFFFAOYSA-N 0.000 claims description 7
239000007864 aqueous solution Substances 0.000 claims description 7
230000002209 hydrophobic effect Effects 0.000 claims description 7
230000003993 interaction Effects 0.000 claims description 7
229910000077 silane Inorganic materials 0.000 claims description 7
229920000936 Agarose Polymers 0.000 claims description 6
102000013566 Plasminogen Human genes 0.000 claims description 6
108010051456 Plasminogen Proteins 0.000 claims description 6
125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 6
229920000193 polymethacrylate Polymers 0.000 claims description 6
125000003277 amino group Chemical group 0.000 claims description 5
229920006037 cross link polymer Polymers 0.000 claims description 5
STVZJERGLQHEKB-UHFFFAOYSA-N ethylene glycol dimethacrylate Chemical group CC(=C)C(=O)OCCOC(=O)C(C)=C STVZJERGLQHEKB-UHFFFAOYSA-N 0.000 claims description 5
102000034238 globular proteins Human genes 0.000 claims description 5
108091005896 globular proteins Proteins 0.000 claims description 5
239000011780 sodium chloride Substances 0.000 claims description 5
238000007334 copolymerization reaction Methods 0.000 claims description 4
238000004108 freeze drying Methods 0.000 claims description 4
210000003296 saliva Anatomy 0.000 claims description 4
125000000217 alkyl group Chemical group 0.000 claims description 3
125000004181 carboxyalkyl group Chemical group 0.000 claims description 3
238000001212 derivatisation Methods 0.000 claims description 3
229920001577 copolymer Polymers 0.000 claims description 2
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims 3
NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 claims 2
239000000243 solution Substances 0.000 claims 2
239000012190 activator Substances 0.000 claims 1
229910000147 aluminium phosphate Inorganic materials 0.000 claims 1
125000003710 aryl alkyl group Chemical group 0.000 claims 1
230000001143 conditioned effect Effects 0.000 claims 1
ZIUHHBKFKCYYJD-UHFFFAOYSA-N n,n'-methylenebisacrylamide Chemical compound C=CC(=O)NCNC(=O)C=C ZIUHHBKFKCYYJD-UHFFFAOYSA-N 0.000 claims 1
238000005277 cation exchange chromatography Methods 0.000 abstract description 3
238000011210 chromatographic step Methods 0.000 abstract 1
238000004191 hydrophobic interaction chromatography Methods 0.000 abstract 1
235000018102 proteins Nutrition 0.000 description 38
210000004027 cell Anatomy 0.000 description 36
239000000047 product Substances 0.000 description 23
239000002609 medium Substances 0.000 description 22
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 9
201000010099 disease Diseases 0.000 description 9
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 9
108010001014 Plasminogen Activators Proteins 0.000 description 8
102000001938 Plasminogen Activators Human genes 0.000 description 8
208000007536 Thrombosis Diseases 0.000 description 8
238000004587 chromatography analysis Methods 0.000 description 8
230000012010 growth Effects 0.000 description 8
210000002966 serum Anatomy 0.000 description 8
238000002560 therapeutic procedure Methods 0.000 description 8
150000001875 compounds Chemical class 0.000 description 7
239000001963 growth medium Substances 0.000 description 7
229940127126 plasminogen activator Drugs 0.000 description 7
239000011534 wash buffer Substances 0.000 description 7
238000011081 inoculation Methods 0.000 description 6
230000010412 perfusion Effects 0.000 description 6
238000002360 preparation method Methods 0.000 description 6
230000002537 thrombolytic effect Effects 0.000 description 6
239000006167 equilibration buffer Substances 0.000 description 5
-1 for example Chemical group 0.000 description 5
210000004962 mammalian cell Anatomy 0.000 description 5
239000008194 pharmaceutical composition Substances 0.000 description 5
229940012957 plasmin Drugs 0.000 description 5
239000000126 substance Substances 0.000 description 5
206010003178 Arterial thrombosis Diseases 0.000 description 4
229960000583 acetic acid Drugs 0.000 description 4
238000005341 cation exchange Methods 0.000 description 4
125000002091 cationic group Chemical group 0.000 description 4
239000003153 chemical reaction reagent Substances 0.000 description 4
239000003636 conditioned culture medium Substances 0.000 description 4
229940079593 drug Drugs 0.000 description 4
239000000825 pharmaceutical preparation Substances 0.000 description 4
238000003860 storage Methods 0.000 description 4
230000003612 virological effect Effects 0.000 description 4
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 3
102000009123 Fibrin Human genes 0.000 description 3
108010073385 Fibrin Proteins 0.000 description 3
BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 3
208000032843 Hemorrhage Diseases 0.000 description 3
VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 3
UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 3
229930195725 Mannitol Natural products 0.000 description 3
102000035195 Peptidases Human genes 0.000 description 3
108091005804 Peptidases Proteins 0.000 description 3
VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 3
206010047249 Venous thrombosis Diseases 0.000 description 3
230000002378 acidificating effect Effects 0.000 description 3
239000003146 anticoagulant agent Substances 0.000 description 3
208000034158 bleeding Diseases 0.000 description 3
230000000740 bleeding effect Effects 0.000 description 3
244000309466 calf Species 0.000 description 3
150000001768 cations Chemical class 0.000 description 3
239000012539 chromatography resin Substances 0.000 description 3
230000003750 conditioning effect Effects 0.000 description 3
238000003795 desorption Methods 0.000 description 3
239000003814 drug Substances 0.000 description 3
239000012149 elution buffer Substances 0.000 description 3
238000000855 fermentation Methods 0.000 description 3
230000004151 fermentation Effects 0.000 description 3
229950003499 fibrin Drugs 0.000 description 3
239000012362 glacial acetic acid Substances 0.000 description 3
239000001257 hydrogen Substances 0.000 description 3
229910052739 hydrogen Inorganic materials 0.000 description 3
230000002779 inactivation Effects 0.000 description 3
239000003112 inhibitor Substances 0.000 description 3
150000002500 ions Chemical class 0.000 description 3
239000000594 mannitol Substances 0.000 description 3
235000010355 mannitol Nutrition 0.000 description 3
125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 3
239000000546 pharmaceutical excipient Substances 0.000 description 3
238000012545 processing Methods 0.000 description 3
238000000926 separation method Methods 0.000 description 3
239000001632 sodium acetate Substances 0.000 description 3
235000017281 sodium acetate Nutrition 0.000 description 3
239000007787 solid Substances 0.000 description 3
238000004114 suspension culture Methods 0.000 description 3
KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 2
239000004365 Protease Substances 0.000 description 2
239000004480 active ingredient Substances 0.000 description 2
230000003698 anagen phase Effects 0.000 description 2
QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
230000004071 biological effect Effects 0.000 description 2
230000015572 biosynthetic process Effects 0.000 description 2
210000004369 blood Anatomy 0.000 description 2
239000008280 blood Substances 0.000 description 2
230000005587 bubbling Effects 0.000 description 2
125000004432 carbon atom Chemical group C* 0.000 description 2
125000002057 carboxymethyl group Chemical group [H]OC(=O)C([H])([H])[*] 0.000 description 2
239000000969 carrier Substances 0.000 description 2
238000004113 cell culture Methods 0.000 description 2
230000010261 cell growth Effects 0.000 description 2
210000004978 chinese hamster ovary cell Anatomy 0.000 description 2
238000003776 cleavage reaction Methods 0.000 description 2
238000010828 elution Methods 0.000 description 2
230000002255 enzymatic effect Effects 0.000 description 2
238000011067 equilibration Methods 0.000 description 2
238000000605 extraction Methods 0.000 description 2
239000000945 filler Substances 0.000 description 2
239000012458 free base Substances 0.000 description 2
239000012737 fresh medium Substances 0.000 description 2
125000000524 functional group Chemical group 0.000 description 2
238000003306 harvesting Methods 0.000 description 2
125000001165 hydrophobic group Chemical group 0.000 description 2
239000004615 ingredient Substances 0.000 description 2
238000001990 intravenous administration Methods 0.000 description 2
238000002955 isolation Methods 0.000 description 2
239000000463 material Substances 0.000 description 2
229940126601 medicinal product Drugs 0.000 description 2
239000000203 mixture Substances 0.000 description 2
229910052760 oxygen Inorganic materials 0.000 description 2
239000001301 oxygen Substances 0.000 description 2
230000017854 proteolysis Effects 0.000 description 2
150000003839 salts Chemical group 0.000 description 2
230000007017 scission Effects 0.000 description 2
SETMGIIITGNLAS-UHFFFAOYSA-N spizofurone Chemical compound O=C1C2=CC(C(=O)C)=CC=C2OC21CC2 SETMGIIITGNLAS-UHFFFAOYSA-N 0.000 description 2
229950001870 spizofurone Drugs 0.000 description 2
230000001225 therapeutic effect Effects 0.000 description 2
229960000103 thrombolytic agent Drugs 0.000 description 2
238000000108 ultra-filtration Methods 0.000 description 2
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
239000012608 weak cation exchange resin Substances 0.000 description 2
CHRJZRDFSQHIFI-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;styrene Chemical compound C=CC1=CC=CC=C1.C=CC1=CC=CC=C1C=C CHRJZRDFSQHIFI-UHFFFAOYSA-N 0.000 description 1
PXFBZOLANLWPMH-UHFFFAOYSA-N 16-Epiaffinine Natural products C1C(C2=CC=CC=C2N2)=C2C(=O)CC2C(=CC)CN(C)C1C2CO PXFBZOLANLWPMH-UHFFFAOYSA-N 0.000 description 1
OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
241000699802 Cricetulus griseus Species 0.000 description 1
102000010911 Enzyme Precursors Human genes 0.000 description 1
108010062466 Enzyme Precursors Proteins 0.000 description 1
241000402754 Erythranthe moschata Species 0.000 description 1
102000008946 Fibrinogen Human genes 0.000 description 1
108010049003 Fibrinogen Proteins 0.000 description 1
235000010469 Glycine max Nutrition 0.000 description 1
244000068988 Glycine max Species 0.000 description 1
206010018852 Haematoma Diseases 0.000 description 1
241000989747 Maba Species 0.000 description 1
241001465754 Metazoa Species 0.000 description 1
BELBBZDIHDAJOR-UHFFFAOYSA-N Phenolsulfonephthalein Chemical compound C1=CC(O)=CC=C1C1(C=2C=CC(O)=CC=2)C2=CC=CC=C2S(=O)(=O)O1 BELBBZDIHDAJOR-UHFFFAOYSA-N 0.000 description 1
108010015078 Pregnancy-Associated alpha 2-Macroglobulins Proteins 0.000 description 1
208000010378 Pulmonary Embolism Diseases 0.000 description 1
102000012479 Serine Proteases Human genes 0.000 description 1
108010022999 Serine Proteases Proteins 0.000 description 1
102000007562 Serum Albumin Human genes 0.000 description 1
108010071390 Serum Albumin Proteins 0.000 description 1
108010023197 Streptokinase Proteins 0.000 description 1
NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
108010022394 Threonine synthase Proteins 0.000 description 1
108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 1
102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 1
239000005862 Whey Substances 0.000 description 1
102000007544 Whey Proteins Human genes 0.000 description 1
108010046377 Whey Proteins Proteins 0.000 description 1
238000010521 absorption reaction Methods 0.000 description 1
239000008351 acetate buffer Substances 0.000 description 1
206010000891 acute myocardial infarction Diseases 0.000 description 1
230000001476 alcoholic effect Effects 0.000 description 1
239000003513 alkali Substances 0.000 description 1
239000003708 ampul Substances 0.000 description 1
238000004458 analytical method Methods 0.000 description 1
230000017531 blood circulation Effects 0.000 description 1
210000004204 blood vessel Anatomy 0.000 description 1
244000309464 bull Species 0.000 description 1
229910052799 carbon Inorganic materials 0.000 description 1
238000011072 cell harvest Methods 0.000 description 1
238000004440 column chromatography Methods 0.000 description 1
230000006378 damage Effects 0.000 description 1
238000000354 decomposition reaction Methods 0.000 description 1
238000011161 development Methods 0.000 description 1
230000018109 developmental process Effects 0.000 description 1
238000009792 diffusion process Methods 0.000 description 1
102000004419 dihydrofolate reductase Human genes 0.000 description 1
239000003085 diluting agent Substances 0.000 description 1
238000010790 dilution Methods 0.000 description 1
239000012895 dilution Substances 0.000 description 1
238000004090 dissolution Methods 0.000 description 1
239000002552 dosage form Substances 0.000 description 1
239000003937 drug carrier Substances 0.000 description 1
230000007717 exclusion Effects 0.000 description 1
239000013604 expression vector Substances 0.000 description 1
229940012952 fibrinogen Drugs 0.000 description 1
239000003527 fibrinolytic agent Substances 0.000 description 1
230000003480 fibrinolytic effect Effects 0.000 description 1
239000002657 fibrous material Substances 0.000 description 1
238000001914 filtration Methods 0.000 description 1
238000011010 flushing procedure Methods 0.000 description 1
230000009931 harmful effect Effects 0.000 description 1
239000001307 helium Substances 0.000 description 1
229910052734 helium Inorganic materials 0.000 description 1
SWQJXJOGLNCZEY-UHFFFAOYSA-N helium atom Chemical compound [He] SWQJXJOGLNCZEY-UHFFFAOYSA-N 0.000 description 1
230000023597 hemostasis Effects 0.000 description 1
238000007912 intraperitoneal administration Methods 0.000 description 1
238000005342 ion exchange Methods 0.000 description 1
239000003456 ion exchange resin Substances 0.000 description 1
229920003303 ion-exchange polymer Polymers 0.000 description 1
125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
239000007788 liquid Substances 0.000 description 1
230000002934 lysing effect Effects 0.000 description 1
101150018863 maa gene Proteins 0.000 description 1
238000002483 medication Methods 0.000 description 1
239000012528 membrane Substances 0.000 description 1
238000012806 monitoring device Methods 0.000 description 1
210000003205 muscle Anatomy 0.000 description 1
208000010125 myocardial infarction Diseases 0.000 description 1
125000004108 n-butyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])* 0.000 description 1
125000001280 n-hexyl group Chemical group C(CCCCC)* 0.000 description 1
125000000740 n-pentyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])* 0.000 description 1
125000004123 n-propyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])* 0.000 description 1
231100000252 nontoxic Toxicity 0.000 description 1
230000003000 nontoxic effect Effects 0.000 description 1
235000015097 nutrients Nutrition 0.000 description 1
229920000620 organic polymer Polymers 0.000 description 1
239000003960 organic solvent Substances 0.000 description 1
210000001672 ovary Anatomy 0.000 description 1
229960003531 phenolsulfonphthalein Drugs 0.000 description 1
125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 1
LFGREXWGYUGZLY-UHFFFAOYSA-N phosphoryl Chemical group [P]=O LFGREXWGYUGZLY-UHFFFAOYSA-N 0.000 description 1
230000004962 physiological condition Effects 0.000 description 1
230000035790 physiological processes and functions Effects 0.000 description 1
239000011148 porous material Substances 0.000 description 1
239000013587 production medium Substances 0.000 description 1
125000001436 propyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
235000004252 protein component Nutrition 0.000 description 1
230000002685 pulmonary effect Effects 0.000 description 1
239000012264 purified product Substances 0.000 description 1
230000001698 pyrogenic effect Effects 0.000 description 1
210000003079 salivary gland Anatomy 0.000 description 1
230000003248 secreting effect Effects 0.000 description 1
239000002002 slurry Substances 0.000 description 1
239000003381 stabilizer Substances 0.000 description 1
238000003756 stirring Methods 0.000 description 1
239000012536 storage buffer Substances 0.000 description 1
229960005202 streptokinase Drugs 0.000 description 1
238000007920 subcutaneous administration Methods 0.000 description 1
KDYFGRWQOYBRFD-UHFFFAOYSA-L succinate(2-) Chemical compound [O-]C(=O)CCC([O-])=O KDYFGRWQOYBRFD-UHFFFAOYSA-L 0.000 description 1
125000000472 sulfonyl group Chemical group *S(*)(=O)=O 0.000 description 1
229910052717 sulfur Inorganic materials 0.000 description 1
239000011593 sulfur Substances 0.000 description 1
230000001629 suppression Effects 0.000 description 1
239000000057 synthetic resin Substances 0.000 description 1
229920003002 synthetic resin Polymers 0.000 description 1
125000000999 tert-butyl group Chemical group [H]C([H])([H])C(*)(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
238000012360 testing method Methods 0.000 description 1
238000011287 therapeutic dose Methods 0.000 description 1
229940126585 therapeutic drug Drugs 0.000 description 1
210000001519 tissue Anatomy 0.000 description 1
230000009466 transformation Effects 0.000 description 1
229960005356 urokinase Drugs 0.000 description 1
230000035899 viability Effects 0.000 description 1
239000002699 waste material 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
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6456—Plasminogen activators
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- 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
- C07K1/16—Extraction; Separation; Purification by chromatography
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides

Landscapes

Chemical & Material Sciences (AREA)
Health & Medical Sciences (AREA)
Organic Chemistry (AREA)
Life Sciences & Earth Sciences (AREA)
Engineering & Computer Science (AREA)
Genetics & Genomics (AREA)
General Health & Medical Sciences (AREA)
Bioinformatics & Cheminformatics (AREA)
Medicinal Chemistry (AREA)
Wood Science & Technology (AREA)
Biochemistry (AREA)
Zoology (AREA)
Biomedical Technology (AREA)
Molecular Biology (AREA)
General Engineering & Computer Science (AREA)
Analytical Chemistry (AREA)
Biophysics (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Microbiology (AREA)
Biotechnology (AREA)
Pharmacology & Pharmacy (AREA)
Veterinary Medicine (AREA)
Public Health (AREA)
Animal Behavior & Ethology (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
General Chemical & Material Sciences (AREA)
Chemical Kinetics & Catalysis (AREA)
Heart & Thoracic Surgery (AREA)
Cardiology (AREA)
Diabetes (AREA)
Hematology (AREA)
Obesity (AREA)
Peptides Or Proteins (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Paper (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Control Of Motors That Do Not Use Commutators (AREA)
Nitrogen And Oxygen Or Sulfur-Condensed Heterocyclic Ring Systems (AREA)
Electric Propulsion And Braking For Vehicles (AREA)
Treatment Of Liquids With Adsorbents In General (AREA)

UA98094695A 1996-02-05 1997-01-31 METHOD FOR PRODUCTION OF rDSPA a1 UA62925C2 (en)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US08/597,059 US5731186A (en)	1996-02-05	1996-02-05	Method for the production of rDSPA α1
PCT/EP1997/000441 WO1997029188A1 (en)	1996-02-05	1997-01-31	METHOD FOR THE PRODUCTION OF rDSPA α1

Publications (1)

Publication Number	Publication Date
UA62925C2 true UA62925C2 (en)	2004-01-15

Family

ID=24389906

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
UA98094695A UA62925C2 (en)	1996-02-05	1997-01-31	METHOD FOR PRODUCTION OF rDSPA a1

Country Status (22)

Country	Link
US (1)	US5731186A (pt)
EP (1)	EP1015568B1 (pt)
JP (1)	JP3805378B2 (pt)
KR (1)	KR100508043B1 (pt)
CN (1)	CN1242059C (pt)
AT (1)	ATE233316T1 (pt)
AU (1)	AU706286B2 (pt)
CZ (1)	CZ294827B6 (pt)
DE (1)	DE69719382T2 (pt)
DK (1)	DK1015568T3 (pt)
ES (1)	ES2193349T3 (pt)
HU (1)	HU223902B1 (pt)
IL (1)	IL124952A (pt)
NO (1)	NO322527B1 (pt)
PL (1)	PL186410B1 (pt)
PT (1)	PT1015568E (pt)
RU (1)	RU2223315C2 (pt)
SK (1)	SK284179B6 (pt)
TW (1)	TW385313B (pt)
UA (1)	UA62925C2 (pt)
WO (1)	WO1997029188A1 (pt)
ZA (1)	ZA97948B (pt)

Families Citing this family (7)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
KR100436655B1 (ko) *	2001-07-25	2004-06-22	(주)엘피스바이오텍	광범위한 단백질에 적용할 수 있는 단백질의 농축 및정제 방법
DE10153601A1 (de) *	2001-11-02	2003-05-22	Paion Gmbh	DSPA zur Behandlung von Schlaganfall
WO2007134617A1 (en) *	2006-05-19	2007-11-29	Paion Deutschland Gmbh	Use of desmodus salivary plasminogen activator (dspa) for treating venous thromboembolism
AR068914A1 (es) *	2007-10-18	2009-12-16	Paion Deutschland Gmbh	Uso de un activador de plasminogeno para la preparacion de un medicamento para el tratamiento de apoplejia
WO2011107299A2 (en) *	2010-04-16	2011-09-09	Paion Deutschland Gmbh	Method for the manufacture of recombinant dspa alpha1
US20120258519A1 (en) *	2011-04-10	2012-10-11	Therapeutic Proteins Inc.	Protein Harvesting
KR102566292B1 (ko)	2015-06-05	2023-08-10	더블유.알. 그레이스 앤드 캄파니-콘.	흡착성 바이오프로세싱 정화제와 이의 제조 및 사용 방법

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DE3512910A1 (de) *	1985-04-11	1986-10-16	Behringwerke Ag, 3550 Marburg	Verfahren zur reinigung von plasminogenaktivatoren
US4721572A (en) *	1985-07-12	1988-01-26	Miles Laboratories, Inc.	Purfication of blood clotting factors and other blood proteins on non-carbohydrate sulfated matrices
US4898825A (en) *	1986-05-07	1990-02-06	Mitsui Toatsu Chemicals, Incorporated	Methods for purification of single-chain and double-chain tissue plasminogen activator
JPS6463378A (en) *	1986-08-11	1989-03-09	Mitsui Toatsu Chemicals	Separation of single stranded tpa and double standard tpa
US4929560A (en) *	1988-02-03	1990-05-29	Damon Biotech, Inc.	Recovery of tissue plasminogen activator
IE69054B1 (en) *	1988-07-20	1996-08-07	Schering Ag	Vampire bat salivary plasminogen activators
ES2085326T3 (es) *	1989-02-13	1996-06-01	Schering Ag	Activador de plasminogeno salivar del murcielago vampiro vpa-alfa1.
DE3943241A1 (de) *	1989-12-22	1991-06-27	Schering Ag	Thrombolytisch wirkendes kombinationspraeparat
US5141862A (en) *	1990-04-17	1992-08-25	Smithkline Beecham Corporation	Method of purifying tpa or plasminogen activator using a tripeptide of the formula: -X-Y-argininal wherein X and Y are selected from the group consisting of pro,phe,trp and tyr

1996
- 1996-02-05 US US08/597,059 patent/US5731186A/en not_active Expired - Lifetime
1997
- 1997-01-31 EP EP97901624A patent/EP1015568B1/en not_active Expired - Lifetime
- 1997-01-31 KR KR10-1998-0706036A patent/KR100508043B1/ko not_active Expired - Lifetime
- 1997-01-31 ES ES97901624T patent/ES2193349T3/es not_active Expired - Lifetime
- 1997-01-31 CZ CZ19982455A patent/CZ294827B6/cs not_active IP Right Cessation
- 1997-01-31 RU RU98116622/12A patent/RU2223315C2/ru active
- 1997-01-31 IL IL12495297A patent/IL124952A/en not_active IP Right Cessation
- 1997-01-31 WO PCT/EP1997/000441 patent/WO1997029188A1/en not_active Ceased
- 1997-01-31 PT PT97901624T patent/PT1015568E/pt unknown
- 1997-01-31 CN CNB971920818A patent/CN1242059C/zh not_active Expired - Lifetime
- 1997-01-31 DE DE69719382T patent/DE69719382T2/de not_active Expired - Lifetime
- 1997-01-31 AT AT97901624T patent/ATE233316T1/de active
- 1997-01-31 PL PL97328146A patent/PL186410B1/pl unknown
- 1997-01-31 HU HU9901029A patent/HU223902B1/hu active IP Right Grant
- 1997-01-31 SK SK1032-98A patent/SK284179B6/sk not_active IP Right Cessation
- 1997-01-31 JP JP52796297A patent/JP3805378B2/ja not_active Expired - Lifetime
- 1997-01-31 AU AU15462/97A patent/AU706286B2/en not_active Expired
- 1997-01-31 UA UA98094695A patent/UA62925C2/uk unknown
- 1997-01-31 DK DK97901624T patent/DK1015568T3/da active
- 1997-02-05 ZA ZA9700948A patent/ZA97948B/xx unknown
- 1997-08-12 TW TW086111545A patent/TW385313B/zh not_active IP Right Cessation
1998
- 1998-08-04 NO NO19983579A patent/NO322527B1/no not_active IP Right Cessation

Also Published As

Publication number	Publication date
NO983579D0 (no)	1998-08-04
HUP9901029A2 (hu)	1999-07-28
CN1242059C (zh)	2006-02-15
PT1015568E (pt)	2003-07-31
ZA97948B (en)	1997-08-19
JP3805378B2 (ja)	2006-08-02
JP2000504565A (ja)	2000-04-18
HK1018795A1 (en)	2000-01-07
HUP9901029A3 (en)	2001-10-29
AU1546297A (en)	1997-08-28
CZ245598A3 (cs)	1999-01-13
DE69719382T2 (de)	2003-11-27
RU2223315C2 (ru)	2004-02-10
US5731186A (en)	1998-03-24
CZ294827B6 (cs)	2005-03-16
DK1015568T3 (da)	2003-06-10
DE69719382D1 (de)	2003-04-03
ATE233316T1 (de)	2003-03-15
SK284179B6 (sk)	2004-10-05
EP1015568B1 (en)	2003-02-26
KR100508043B1 (ko)	2005-12-21
CN1210559A (zh)	1999-03-10
NO322527B1 (no)	2006-10-16
ES2193349T3 (es)	2003-11-01
TW385313B (en)	2000-03-21
HU223902B1 (hu)	2005-03-29
EP1015568A1 (en)	2000-07-05
IL124952A (en)	2002-08-14
KR19990082306A (ko)	1999-11-25
AU706286B2 (en)	1999-06-10
PL328146A1 (en)	1999-01-18
IL124952A0 (en)	1999-01-26
SK103298A3 (en)	1999-03-12
NO983579L (no)	1998-10-05
PL186410B1 (pl)	2004-01-30
WO1997029188A1 (en)	1997-08-14

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US4743680A (en)	1988-05-10	Method for purifying antihemophilic factor
CA2024667C (en)	2001-07-31	Process for preparing a concentrate of blood coagulation factor viii-von willebrand factor complex from total plasma
AU2003244850B2 (en)	2009-06-25	Processes for the preparation of fibrinogen
CA2006684C (en)	1996-12-17	Monoclonal antibody against protein c
JP2001513088A (ja)	2001-08-28	カチオン交換クロマトグラフィーによるフォンビルブラント因子の精製
US4774323A (en)	1988-09-27	Purification of von Willebrand Factor solutions using gel permeation chromatography
CN108660126A (zh)	2018-10-16	一种冻干人凝血酶的制备工艺
UA62925C2 (en)	2004-01-15	METHOD FOR PRODUCTION OF rDSPA a1
US5006642A (en)	1991-04-09	Purification of von Willebrand Factor by affinity chromatography
US4847362A (en)	1989-07-11	Method for purifying antihemophilic factor
US20020019036A1 (en)	2002-02-14	Von willebrand factor derivatives and methods of isolating proteins that bind to von willebrand factor
JPH0223158B2 (pt)	1990-05-23
CA2245554C (en)	2006-07-04	Method for the production of rdspa .alpha.1
JP2001506987A (ja)	2001-05-29	フォンビルブラント因子誘導体及びタンパク質の単離法
HK1018795B (en)	2006-08-04	METHOD FOR THE PRODUCTION OF rDSPAα I
SU767121A1 (ru)	1980-09-30	Способ выделени и очистки трипсина и химотрипсина
JPH01304881A (ja)	1989-12-08	ウロキナーゼ前駆体の製造方法