JPH0532025B2 - - Google Patents
Info
- Publication number
- JPH0532025B2 JPH0532025B2 JP60079300A JP7930085A JPH0532025B2 JP H0532025 B2 JPH0532025 B2 JP H0532025B2 JP 60079300 A JP60079300 A JP 60079300A JP 7930085 A JP7930085 A JP 7930085A JP H0532025 B2 JPH0532025 B2 JP H0532025B2
- Authority
- JP
- Japan
- Prior art keywords
- cells
- kym
- mutant strain
- mutant
- culture
- 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
- 210000004027 cell Anatomy 0.000 claims description 56
- 238000013019 agitation Methods 0.000 claims description 12
- 238000007667 floating Methods 0.000 claims description 12
- 210000000349 chromosome Anatomy 0.000 claims description 10
- 206010028980 Neoplasm Diseases 0.000 claims description 5
- 229920003023 plastic Polymers 0.000 claims description 5
- 206010061692 Benign muscle neoplasm Diseases 0.000 claims description 4
- 201000004458 Myoma Diseases 0.000 claims description 4
- 108010001014 Plasminogen Activators Proteins 0.000 claims description 4
- 102000001938 Plasminogen Activators Human genes 0.000 claims description 4
- 229940127126 plasminogen activator Drugs 0.000 claims description 4
- 239000003636 conditioned culture medium Substances 0.000 claims description 3
- 241000699800 Cricetinae Species 0.000 claims description 2
- 241000699660 Mus musculus Species 0.000 claims description 2
- 230000001464 adherent effect Effects 0.000 claims description 2
- 238000007796 conventional method Methods 0.000 claims description 2
- 230000002559 cytogenic effect Effects 0.000 claims description 2
- 238000009826 distribution Methods 0.000 claims description 2
- 238000011580 nude mouse model Methods 0.000 claims description 2
- 206010011732 Cyst Diseases 0.000 claims 1
- 208000031513 cyst Diseases 0.000 claims 1
- 239000002609 medium Substances 0.000 description 16
- 230000000694 effects Effects 0.000 description 11
- 239000000126 substance Substances 0.000 description 9
- 239000000243 solution Substances 0.000 description 7
- 206010003497 Asphyxia Diseases 0.000 description 6
- 238000011160 research Methods 0.000 description 6
- 239000000725 suspension Substances 0.000 description 6
- 208000007536 Thrombosis Diseases 0.000 description 5
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 5
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 5
- 239000000853 adhesive Substances 0.000 description 5
- 230000001070 adhesive effect Effects 0.000 description 5
- 210000004881 tumor cell Anatomy 0.000 description 5
- 229960005356 urokinase Drugs 0.000 description 5
- 102000009123 Fibrin Human genes 0.000 description 4
- 108010073385 Fibrin Proteins 0.000 description 4
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 4
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 229950003499 fibrin Drugs 0.000 description 4
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 4
- 201000001441 melanoma Diseases 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 239000012679 serum free medium Substances 0.000 description 4
- 210000001519 tissue Anatomy 0.000 description 4
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 206010006187 Breast cancer Diseases 0.000 description 3
- 208000026310 Breast neoplasm Diseases 0.000 description 3
- 201000009030 Carcinoma Diseases 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 102000003886 Glycoproteins Human genes 0.000 description 3
- 108090000288 Glycoproteins Proteins 0.000 description 3
- 102000013566 Plasminogen Human genes 0.000 description 3
- 108010051456 Plasminogen Proteins 0.000 description 3
- 239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 3
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 3
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 description 3
- 238000000862 absorption spectrum Methods 0.000 description 3
- 150000001413 amino acids Chemical class 0.000 description 3
- 238000010586 diagram Methods 0.000 description 3
- 239000012091 fetal bovine serum Substances 0.000 description 3
- OOYGSFOGFJDDHP-KMCOLRRFSA-N kanamycin A sulfate Chemical compound OS(O)(=O)=O.O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N OOYGSFOGFJDDHP-KMCOLRRFSA-N 0.000 description 3
- 229960002064 kanamycin sulfate Drugs 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 229960000187 tissue plasminogen activator Drugs 0.000 description 3
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 2
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 230000005526 G1 to G0 transition Effects 0.000 description 2
- 206010062713 Haemorrhagic diathesis Diseases 0.000 description 2
- 101000766306 Homo sapiens Serotransferrin Proteins 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- 102000004877 Insulin Human genes 0.000 description 2
- 108090001061 Insulin Proteins 0.000 description 2
- 101710093543 Probable non-specific lipid-transfer protein Proteins 0.000 description 2
- 108010023197 Streptokinase Proteins 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 239000003114 blood coagulation factor Substances 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 210000002889 endothelial cell Anatomy 0.000 description 2
- 208000031169 hemorrhagic disease Diseases 0.000 description 2
- 238000009776 industrial production Methods 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 229940125396 insulin Drugs 0.000 description 2
- 238000000034 method Methods 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- XNSAINXGIQZQOO-SRVKXCTJSA-N protirelin Chemical compound NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H]1NC(=O)CC1)CC1=CN=CN1 XNSAINXGIQZQOO-SRVKXCTJSA-N 0.000 description 2
- 229940082569 selenite Drugs 0.000 description 2
- MCAHWIHFGHIESP-UHFFFAOYSA-L selenite(2-) Chemical compound [O-][Se]([O-])=O MCAHWIHFGHIESP-UHFFFAOYSA-L 0.000 description 2
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 2
- 235000017557 sodium bicarbonate Nutrition 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 229960005202 streptokinase Drugs 0.000 description 2
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 1
- ONZHLZFZUVGRCW-UHFFFAOYSA-N 2-[(2-phenylmethoxyphenyl)methylamino]-1-[3-(trifluoromethyl)phenyl]ethanol Chemical compound C=1C=CC(C(F)(F)F)=CC=1C(O)CNCC1=CC=CC=C1OCC1=CC=CC=C1 ONZHLZFZUVGRCW-UHFFFAOYSA-N 0.000 description 1
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 108010039627 Aprotinin Proteins 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 108010062580 Concanavalin A Proteins 0.000 description 1
- 102000002322 Egg Proteins Human genes 0.000 description 1
- 108010000912 Egg Proteins Proteins 0.000 description 1
- 102000016359 Fibronectins Human genes 0.000 description 1
- 108010067306 Fibronectins Proteins 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 239000012980 RPMI-1640 medium Substances 0.000 description 1
- 206010039491 Sarcoma Diseases 0.000 description 1
- UIIMBOGNXHQVGW-DEQYMQKBSA-M Sodium bicarbonate-14C Chemical compound [Na+].O[14C]([O-])=O UIIMBOGNXHQVGW-DEQYMQKBSA-M 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 229960004405 aprotinin Drugs 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 239000007640 basal medium Substances 0.000 description 1
- 229940019700 blood coagulation factors Drugs 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 229910002092 carbon dioxide Inorganic materials 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 235000014103 egg white Nutrition 0.000 description 1
- 210000000969 egg white Anatomy 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 239000003527 fibrinolytic agent Substances 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 206010073071 hepatocellular carcinoma Diseases 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000002808 molecular sieve Substances 0.000 description 1
- 238000010899 nucleation Methods 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 229940012957 plasmin Drugs 0.000 description 1
- 229920000729 poly(L-lysine) polymer Polymers 0.000 description 1
- ZNNZYHKDIALBAK-UHFFFAOYSA-M potassium thiocyanate Chemical compound [K+].[S-]C#N ZNNZYHKDIALBAK-UHFFFAOYSA-M 0.000 description 1
- 229940116357 potassium thiocyanate Drugs 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 238000000926 separation method Methods 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
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 229960000103 thrombolytic agent Drugs 0.000 description 1
- 210000004291 uterus Anatomy 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP60079300A JPS611382A (ja) | 1985-04-16 | 1985-04-16 | 変異株kym−a |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP60079300A JPS611382A (ja) | 1985-04-16 | 1985-04-16 | 変異株kym−a |
Related Parent Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP59013397A Division JPS60158115A (ja) | 1984-01-30 | 1984-01-30 | プラズミノーゲンアクチベーターの製造法 |
Publications (2)
Publication Number | Publication Date |
---|---|
JPS611382A JPS611382A (ja) | 1986-01-07 |
JPH0532025B2 true JPH0532025B2 (ko) | 1993-05-14 |
Family
ID=13685992
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP60079300A Granted JPS611382A (ja) | 1985-04-16 | 1985-04-16 | 変異株kym−a |
Country Status (1)
Country | Link |
---|---|
JP (1) | JPS611382A (ko) |
-
1985
- 1985-04-16 JP JP60079300A patent/JPS611382A/ja active Granted
Also Published As
Publication number | Publication date |
---|---|
JPS611382A (ja) | 1986-01-07 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
KR900008740B1 (ko) | 혈청-비의존성 사람 세포주 및 이의 돌연변이 세포주를 제조하는 방법 | |
Chiplonkar et al. | Applications of alkaline protease from Conidiobolus in animal cell culture | |
Gronow et al. | Production of human plasminogen activators by cell culture | |
US11220666B2 (en) | Bacterial strain clostridium histolyticum and methods of use thereof | |
JPH0532025B2 (ko) | ||
JPS6119486A (ja) | 組織プラスミノ−ゲンアクチベ−タ−、その製法及びその利用 | |
EP0163751B1 (en) | Process for the preparation of a plasminogen activator | |
KR0180103B1 (ko) | 바실러스 서브틸리스 속 균주 유래의 혈전용해효소 | |
JPH0569506B2 (ko) | ||
JP3133148B2 (ja) | ヒト細胞性フィブロネクチン、その製造法及び細胞株 | |
JPS60231611A (ja) | プラズミノ−ゲンアクチベ−タ−の製造法 | |
EP0253314B1 (en) | Peptidase and process for producing the same | |
JP2879906B2 (ja) | プロコラゲナーゼの製造方法 | |
JP4190753B2 (ja) | 血管新生阻害活性をもつプラスミノゲン断片およびその生成を導く化合物の探索方法 | |
CA1177424A (en) | Composition for cell culture | |
KR980009454A (ko) | 바실러스속 균주 유래의 혈전용해효소 | |
JPS62158220A (ja) | 変異株kym−e | |
JPS6156997B2 (ko) | ||
JPS62153221A (ja) | ヒト子宮筋正常組織由来樹立化細胞kw株及びその培養によるプラスミノ−ゲンアクチベ−タ−の製造法 | |
Muranova et al. | Anti-adhesive property of the plasmin/plasminogen system: the use of plasmin (ogen) for cell detachment and disaggregation in cell culture technique | |
JPH012573A (ja) | カルボキシペプチダーゼの製造方法 | |
JPH05310796A (ja) | 新規なヒト細胞性フィブロネクチン | |
JPH01157384A (ja) | 非会合の組織プラスミノーゲン活性化因子を培養細胞から高収率で得る方法 | |
JPS6352879A (ja) | 組織性プラスミノ−ゲンアクチベ−タ前駆体 | |
JPS60248178A (ja) | ヒト血管内皮細胞の培養方法 |