JPH04500010A - ｔ―ＰＡ―変異体ＧＫ１Ｌ - Google Patents
ｔ―ＰＡ―変異体ＧＫ１ＬInfo
- Publication number
- JPH04500010A JPH04500010A JP2511463A JP51146390A JPH04500010A JP H04500010 A JPH04500010 A JP H04500010A JP 2511463 A JP2511463 A JP 2511463A JP 51146390 A JP51146390 A JP 51146390A JP H04500010 A JPH04500010 A JP H04500010A
- Authority
- JP
- Japan
- Prior art keywords
- recombinant dna
- regions
- gene
- protein
- cells
- 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.)
- Granted
Links
- 108090000623 proteins and genes Proteins 0.000 claims description 24
- 102000004169 proteins and genes Human genes 0.000 claims description 20
- 239000013612 plasmid Substances 0.000 claims description 17
- 108020004511 Recombinant DNA Proteins 0.000 claims description 13
- 239000013598 vector Substances 0.000 claims description 11
- 108010039627 Aprotinin Proteins 0.000 claims description 10
- 229960004405 aprotinin Drugs 0.000 claims description 10
- 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 claims description 10
- 238000004519 manufacturing process Methods 0.000 claims description 9
- 239000002609 medium Substances 0.000 claims description 9
- 238000000034 method Methods 0.000 claims description 8
- 231100000350 mutagenesis Toxicity 0.000 claims description 6
- 238000002703 mutagenesis Methods 0.000 claims description 6
- 238000012217 deletion Methods 0.000 claims description 4
- 230000037430 deletion Effects 0.000 claims description 4
- 230000003480 fibrinolytic effect Effects 0.000 claims description 4
- 239000001963 growth medium Substances 0.000 claims description 4
- 108020004414 DNA Proteins 0.000 claims description 3
- 101100278853 Mus musculus Dhfr gene Proteins 0.000 claims description 2
- 230000007850 degeneration Effects 0.000 claims description 2
- 239000003527 fibrinolytic agent Substances 0.000 claims description 2
- 230000002068 genetic effect Effects 0.000 claims description 2
- 108050006955 Tissue-type plasminogen activator Proteins 0.000 claims 4
- 102100033571 Tissue-type plasminogen activator Human genes 0.000 claims 3
- 108700024394 Exon Proteins 0.000 claims 1
- 101150105115 PA gene Proteins 0.000 claims 1
- 125000003275 alpha amino acid group Chemical group 0.000 claims 1
- 238000011084 recovery Methods 0.000 claims 1
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 33
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 description 31
- 229960000187 tissue plasminogen activator Drugs 0.000 description 31
- 210000004027 cell Anatomy 0.000 description 28
- 230000000694 effects Effects 0.000 description 16
- 239000006228 supernatant Substances 0.000 description 14
- 102000009123 Fibrin Human genes 0.000 description 12
- 108010073385 Fibrin Proteins 0.000 description 12
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 12
- 229950003499 fibrin Drugs 0.000 description 12
- 239000012634 fragment Substances 0.000 description 12
- 239000002773 nucleotide Substances 0.000 description 10
- 125000003729 nucleotide group Chemical group 0.000 description 10
- 102000013566 Plasminogen Human genes 0.000 description 9
- 108010051456 Plasminogen Proteins 0.000 description 9
- 102000008946 Fibrinogen Human genes 0.000 description 8
- 108010049003 Fibrinogen Proteins 0.000 description 8
- 230000003197 catalytic effect Effects 0.000 description 8
- 229940012952 fibrinogen Drugs 0.000 description 8
- 239000002299 complementary DNA Substances 0.000 description 7
- 238000003776 cleavage reaction Methods 0.000 description 5
- 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 4
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 230000007017 scission Effects 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 108091028026 C-DNA Proteins 0.000 description 3
- 102000012479 Serine Proteases Human genes 0.000 description 3
- 108010022999 Serine Proteases Proteins 0.000 description 3
- 229940098773 bovine serum albumin Drugs 0.000 description 3
- 238000009396 hybridization Methods 0.000 description 3
- 229940012957 plasmin Drugs 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 206010034133 Pathogen resistance Diseases 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 108091023045 Untranslated Region Proteins 0.000 description 2
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 2
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 2
- 150000001413 amino acids Chemical group 0.000 description 2
- 229960000723 ampicillin Drugs 0.000 description 2
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 2
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 2
- 239000003593 chromogenic compound Substances 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- VNWKTOKETHGBQD-UHFFFAOYSA-N methane Chemical compound C VNWKTOKETHGBQD-UHFFFAOYSA-N 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 231100000219 mutagenic Toxicity 0.000 description 2
- 230000003505 mutagenic effect Effects 0.000 description 2
- 230000008488 polyadenylation Effects 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 238000001890 transfection Methods 0.000 description 2
- 229960005356 urokinase Drugs 0.000 description 2
- YRNWIFYIFSBPAU-UHFFFAOYSA-N 4-[4-(dimethylamino)phenyl]-n,n-dimethylaniline Chemical compound C1=CC(N(C)C)=CC=C1C1=CC=C(N(C)C)C=C1 YRNWIFYIFSBPAU-UHFFFAOYSA-N 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 102000018832 Cytochromes Human genes 0.000 description 1
- 108010052832 Cytochromes Proteins 0.000 description 1
- 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 1
- 238000002965 ELISA Methods 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 102000016359 Fibronectins Human genes 0.000 description 1
- 108010067306 Fibronectins Proteins 0.000 description 1
- 229920001917 Ficoll Polymers 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 102100021519 Hemoglobin subunit beta Human genes 0.000 description 1
- 108091005904 Hemoglobin subunit beta Proteins 0.000 description 1
- 101500025419 Homo sapiens Epidermal growth factor Proteins 0.000 description 1
- 101000801481 Homo sapiens Tissue-type plasminogen activator Proteins 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 1
- 108091026898 Leader sequence (mRNA) Proteins 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 101500025418 Mus musculus Epidermal growth factor Proteins 0.000 description 1
- 102000003505 Myosin Human genes 0.000 description 1
- 108060008487 Myosin Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 101710149086 Nuclease S1 Proteins 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- 102000009097 Phosphorylases Human genes 0.000 description 1
- 108010073135 Phosphorylases Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 108010023197 Streptokinase Proteins 0.000 description 1
- ULUAUXLGCMPNKK-UHFFFAOYSA-N Sulfobutanedioic acid Chemical compound OC(=O)CC(C(O)=O)S(O)(=O)=O ULUAUXLGCMPNKK-UHFFFAOYSA-N 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 108091036066 Three prime untranslated region Proteins 0.000 description 1
- 208000007536 Thrombosis Diseases 0.000 description 1
- 101710162629 Trypsin inhibitor Proteins 0.000 description 1
- 229940122618 Trypsin inhibitor Drugs 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000008186 active pharmaceutical agent Substances 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 208000031513 cyst Diseases 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000003113 dilution method Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 238000009585 enzyme analysis Methods 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 230000005284 excitation Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 230000020764 fibrinolysis Effects 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 239000000499 gel 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
- 239000003292 glue Substances 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 230000023597 hemostasis Effects 0.000 description 1
- 102000047823 human PLAT Human genes 0.000 description 1
- 229940116978 human epidermal growth factor Drugs 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 210000003127 knee Anatomy 0.000 description 1
- 230000002934 lysing effect Effects 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
- 239000011159 matrix material Substances 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 229960000485 methotrexate Drugs 0.000 description 1
- WLGOTMXHWBRTJA-GACYYNSASA-N murodermin Chemical compound C([C@H]1C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@H](C(=O)N[C@H](C(NCC(=O)N1)=O)[C@@H](C)CC)C(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H]1NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC=2C=CC(O)=CC=2)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CC=2NC=NC=2)NC(=O)[C@H](CCSC)NC(=O)[C@@H]2CSSC[C@@H](C(=O)N3CCC[C@H]3C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CC(O)=O)C(=O)NCC(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@H](C(N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)NCC(=O)N[C@H](C(=O)N2)C(C)C)=O)CSSC1)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C1=CC=C(O)C=C1 WLGOTMXHWBRTJA-GACYYNSASA-N 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- GVUGOAYIVIDWIO-UFWWTJHBSA-N nepidermin Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CS)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CS)NC(=O)[C@H](C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C(C)C)C(C)C)C1=CC=C(O)C=C1 GVUGOAYIVIDWIO-UFWWTJHBSA-N 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 102000013415 peroxidase activity proteins Human genes 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 230000000379 polymerizing effect Effects 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 229940016590 sarkosyl Drugs 0.000 description 1
- 108700004121 sarkosyl Proteins 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 239000006152 selective media Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- KSAVQLQVUXSOCR-UHFFFAOYSA-M sodium lauroyl sarcosinate Chemical compound [Na+].CCCCCCCCCCCC(=O)N(C)CC([O-])=O KSAVQLQVUXSOCR-UHFFFAOYSA-M 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 229960005202 streptokinase Drugs 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 235000013616 tea Nutrition 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 238000007070 tosylation reaction Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- 229920002554 vinyl polymer Polymers 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 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
- C12N9/6459—Plasminogen activators t-plasminogen activator (3.4.21.68), i.e. tPA
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A61P7/02—Antithrombotic agents; Anticoagulants; Platelet aggregation inhibitors
-
- 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)
- C12Y304/21069—Protein C activated (3.4.21.69)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Life Sciences & Earth Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Diabetes (AREA)
- Public Health (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Hematology (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Veterinary Medicine (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Oscillators With Electromechanical Resonators (AREA)
- Transition And Organic Metals Composition Catalysts For Addition Polymerization (AREA)
- Curing Cements, Concrete, And Artificial Stone (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE3927865.4 | 1989-08-23 | ||
| DE3927865A DE3927865A1 (de) | 1989-08-23 | 1989-08-23 | T-pa-mutante gk1l |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH04500010A true JPH04500010A (ja) | 1992-01-09 |
| JPH0571228B2 JPH0571228B2 (en22) | 1993-10-06 |
Family
ID=6387718
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2511463A Granted JPH04500010A (ja) | 1989-08-23 | 1990-08-22 | ｔ―ＰＡ―変異体ＧＫ１Ｌ |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US5223422A (en22) |
| EP (1) | EP0440763B1 (en22) |
| JP (1) | JPH04500010A (en22) |
| AT (1) | ATE120236T1 (en22) |
| DE (2) | DE3927865A1 (en22) |
| WO (1) | WO1991002798A2 (en22) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2002020802A1 (fr) * | 2000-09-04 | 2002-03-14 | Hunan Royal Biotech | Lignee cellulaire exprimant un activateur de plasminogene tissulaire humain mutant, procede de recombinaison et procede de preparation de la proteine exprimee |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0231624B1 (en) * | 1985-12-20 | 1993-01-27 | The Upjohn Company | Tissue plasminogen activator (tpa) analogs |
-
1989
- 1989-08-23 DE DE3927865A patent/DE3927865A1/de not_active Withdrawn
-
1990
- 1990-08-22 JP JP2511463A patent/JPH04500010A/ja active Granted
- 1990-08-22 WO PCT/EP1990/001401 patent/WO1991002798A2/de active IP Right Grant
- 1990-08-22 US US07/671,776 patent/US5223422A/en not_active Expired - Fee Related
- 1990-08-22 AT AT90912217T patent/ATE120236T1/de not_active IP Right Cessation
- 1990-08-22 EP EP90912217A patent/EP0440763B1/de not_active Expired - Lifetime
- 1990-08-22 DE DE59008764T patent/DE59008764D1/de not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| DE3927865A1 (de) | 1991-02-28 |
| WO1991002798A2 (de) | 1991-03-07 |
| US5223422A (en) | 1993-06-29 |
| ATE120236T1 (de) | 1995-04-15 |
| EP0440763A1 (de) | 1991-08-14 |
| DE59008764D1 (de) | 1995-04-27 |
| EP0440763B1 (de) | 1995-03-22 |
| JPH0571228B2 (en22) | 1993-10-06 |
| WO1991002798A3 (de) | 1991-04-04 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2575369B2 (ja) | 新規ペプチドのプラスミノ−ゲンアクチベ−タ− | |
| JP4451514B2 (ja) | 血液凝固第ｖｉｉ因子改変体 | |
| EP0370036B1 (en) | Modified factor vii/viia | |
| KR101529743B1 (ko) | 재조합적으로 변형된 플라스민 | |
| JP2991769B2 (ja) | セルピン抵抗性キモトリプシン スーパーフアミリー プロテアーゼ、特にＰＡＩ―１抵抗性ｔ―ＰＡ、相補的阻害剤変異株；組成；遺伝子；発現 | |
| JP2610783B2 (ja) | ポリクリングルプラスミノーゲン活性化因子をコードする遺伝子およびそれを含有するベクター | |
| JP2713467B2 (ja) | バンパイアバット唾液プラスミノーゲン賦活体 | |
| JPH06501616A (ja) | 同起源インヒビターによる阻害に対して抵抗性のキモトリプシンスーパーファミリーのセリンプロテアーゼ変異株及びそれをコードする遺伝子、ならびにセリンプロテアーゼインヒビター変異株及びそれをコードする遺伝子 | |
| WO1988009811A1 (en) | Proteins and derivatives thereof | |
| AU2009318554B2 (en) | Fusion collagenase to which affinity tag is attached, and method for producing same | |
| IE57699B1 (en) | Synthesis of tissue plasminogen activator(tpa)by yeast | |
| US4968626A (en) | DNA sequence coding for protein C | |
| JP2003504082A (ja) | エカリンポリペプチド、エカリンをコードするポリヌクレオチド、及びその利用のための方法 | |
| JP2728240B2 (ja) | ヒトプロテインｃ変異体及びその製造方法 | |
| Yu et al. | Expression and purification of ancrod, an anticoagulant drug, in Pichia pastoris | |
| JPH03502526A (ja) | ヒトプロウロキナーゼの製造 | |
| JPH04500010A (ja) | ｔ―ＰＡ―変異体ＧＫ１Ｌ | |
| Davami et al. | Expression of a novel chimeric truncated t‐PA in CHO cells based on in silico experiments | |
| JP7171434B2 (ja) | 遺伝的改変酵母細胞と血栓特異的ストレプトキナーゼ製造改良プロセス | |
| JPH04506897A (ja) | 修飾されたクリングルドメインを有する血栓溶解剤 | |
| CN102559645B (zh) | 一种人阴离子胰蛋白酶突变体 | |
| WO2008046256A1 (fr) | Hemocoagulase | |
| JP2859297B2 (ja) | トロンビン阻害活性を有するポリペプチドおよびその製造法 | |
| Fischer et al. | Purification of recombinant human coagulation factors II and IX and protein S expressed in recombinant Vaccinia virus-infected Vero cells | |
| EP0316068A1 (en) | Modified low molecular weight plasminogen activator and method of preparation |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| LAPS | Cancellation because of no payment of annual fees |