DD298426A5 - Verfahren zur herstellung von neuen plasmiden und deren verwendung bei der gewinnung eines plasminogenaktivators - Google Patents

Verfahren zur herstellung von neuen plasmiden und deren verwendung bei der gewinnung eines plasminogenaktivators Download PDF

Info

Publication number: DD298426A5
Authority: DD; German Democratic Republic
Prior art keywords: plasmid; coli; rscu; plasmids; structural gene
Prior art date: 1989-07-19

Application number

DD90342894A

Other languages

German (de)

English (en)

Inventor

Regina E Brigelius-Flohe

Leopold Flohe

Wolfgang Hillen

Gerd Steffens

Wolfgang Strassburger

Martin R F Wilhelm

Original Assignee

��@��k��

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.)

1989-07-19

Filing date

1990-07-18

Publication date

1992-02-20

1990-07-18 Application filed by ��@��k�� filed Critical ��@��k��

1992-02-20 Publication of DD298426A5 publication Critical patent/DD298426A5/de

Links

108010001014 Plasminogen Activators Proteins 0.000 title claims abstract description 6
102000001938 Plasminogen Activators Human genes 0.000 title claims abstract description 6
229940127126 plasminogen activator Drugs 0.000 title claims abstract description 6
238000004519 manufacturing process Methods 0.000 title claims description 9
239000013612 plasmid Substances 0.000 claims abstract description 130
108090000623 proteins and genes Proteins 0.000 claims abstract description 93
102000004169 proteins and genes Human genes 0.000 claims abstract description 52
239000002243 precursor Substances 0.000 claims abstract description 40
241000588724 Escherichia coli Species 0.000 claims abstract description 31
108091081024 Start codon Proteins 0.000 claims abstract description 13
108090000435 Urokinase-type plasminogen activator Proteins 0.000 claims abstract description 7
102000003990 Urokinase-type plasminogen activator Human genes 0.000 claims abstract description 7
241000588921 Enterobacteriaceae Species 0.000 claims abstract description 5
238000002360 preparation method Methods 0.000 claims abstract 4
239000012634 fragment Substances 0.000 claims description 56
239000002773 nucleotide Substances 0.000 claims description 31
125000003729 nucleotide group Chemical group 0.000 claims description 31
241001646716 Escherichia coli K-12 Species 0.000 claims description 29
238000010367 cloning Methods 0.000 claims description 15
238000000034 method Methods 0.000 claims description 10
230000001580 bacterial effect Effects 0.000 claims description 4
238000005520 cutting process Methods 0.000 claims description 4
238000013518 transcription Methods 0.000 claims description 4
230000035897 transcription Effects 0.000 claims description 4
238000011049 filling Methods 0.000 claims description 2
125000000539 amino acid group Chemical group 0.000 claims 1
238000011084 recovery Methods 0.000 claims 1
238000003776 cleavage reaction Methods 0.000 abstract description 7
230000007017 scission Effects 0.000 abstract description 7
108010073863 saruplase Proteins 0.000 abstract description 5
108091028043 Nucleic acid sequence Proteins 0.000 abstract description 3
235000018102 proteins Nutrition 0.000 description 44
238000010276 construction Methods 0.000 description 24
239000002609 medium Substances 0.000 description 23
229960000723 ampicillin Drugs 0.000 description 18
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 18
210000004027 cell Anatomy 0.000 description 18
230000006698 induction Effects 0.000 description 18
230000000694 effects Effects 0.000 description 17
230000009466 transformation Effects 0.000 description 16
238000012258 culturing Methods 0.000 description 13
238000010348 incorporation Methods 0.000 description 13
229940024606 amino acid Drugs 0.000 description 10
235000001014 amino acid Nutrition 0.000 description 10
150000001413 amino acids Chemical class 0.000 description 10
239000004098 Tetracycline Substances 0.000 description 9
229960002180 tetracycline Drugs 0.000 description 9
229930101283 tetracycline Natural products 0.000 description 9
235000019364 tetracycline Nutrition 0.000 description 9
150000003522 tetracyclines Chemical class 0.000 description 9
SXOUIMVOMIGLHO-AATRIKPKSA-N (E)-3-(indol-2-yl)acrylic acid Chemical compound C1=CC=C2NC(/C=C/C(=O)O)=CC2=C1 SXOUIMVOMIGLHO-AATRIKPKSA-N 0.000 description 8
108091034117 Oligonucleotide Proteins 0.000 description 8
PLVPPLCLBIEYEA-UHFFFAOYSA-N indoleacrylic acid Natural products C1=CC=C2C(C=CC(=O)O)=CNC2=C1 PLVPPLCLBIEYEA-UHFFFAOYSA-N 0.000 description 8
BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 8
230000003287 optical effect Effects 0.000 description 8
238000012360 testing method Methods 0.000 description 8
108010054576 Deoxyribonuclease EcoRI Proteins 0.000 description 7
238000000246 agarose gel electrophoresis Methods 0.000 description 7
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Natural products CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
241000894006 Bacteria Species 0.000 description 6
108020004705 Codon Proteins 0.000 description 6
102000003960 Ligases Human genes 0.000 description 6
108090000364 Ligases Proteins 0.000 description 6
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
239000013613 expression plasmid Substances 0.000 description 6
229940012957 plasmin Drugs 0.000 description 6
230000004913 activation Effects 0.000 description 5
239000006285 cell suspension Substances 0.000 description 5
238000000855 fermentation Methods 0.000 description 5
230000004151 fermentation Effects 0.000 description 5
239000000499 gel Substances 0.000 description 5
239000000758 substrate Substances 0.000 description 5
108020004414 DNA Proteins 0.000 description 4
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 4
230000015572 biosynthetic process Effects 0.000 description 4
238000006243 chemical reaction Methods 0.000 description 4
230000001105 regulatory effect Effects 0.000 description 4
239000013598 vector Substances 0.000 description 4
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
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 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
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
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
102000016943 Muramidase Human genes 0.000 description 3
108010014251 Muramidase Proteins 0.000 description 3
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 3
239000007983 Tris buffer Substances 0.000 description 3
JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 3
239000000872 buffer Substances 0.000 description 3
229950003499 fibrin Drugs 0.000 description 3
239000008103 glucose Substances 0.000 description 3
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 description 3
PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 3
229960000274 lysozyme Drugs 0.000 description 3
235000010335 lysozyme Nutrition 0.000 description 3
239000004325 lysozyme Substances 0.000 description 3
238000000746 purification Methods 0.000 description 3
239000011780 sodium chloride Substances 0.000 description 3
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 3
229960005356 urokinase Drugs 0.000 description 3
239000004475 Arginine Substances 0.000 description 2
108010077805 Bacterial Proteins Proteins 0.000 description 2
102000004594 DNA Polymerase I Human genes 0.000 description 2
108010017826 DNA Polymerase I Proteins 0.000 description 2
102000004190 Enzymes Human genes 0.000 description 2
108090000790 Enzymes Proteins 0.000 description 2
108010024636 Glutathione Proteins 0.000 description 2
239000004471 Glycine Substances 0.000 description 2
ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 2
KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
239000001888 Peptone Substances 0.000 description 2
108010080698 Peptones Proteins 0.000 description 2
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
238000002835 absorbance Methods 0.000 description 2
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
229940041514 candida albicans extract Drugs 0.000 description 2
238000004587 chromatography analysis Methods 0.000 description 2
238000012217 deletion Methods 0.000 description 2
230000037430 deletion Effects 0.000 description 2
XBDQKXXYIPTUBI-UHFFFAOYSA-N dimethylselenoniopropionate Natural products CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 description 2
229940088598 enzyme Drugs 0.000 description 2
DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 2
238000001502 gel electrophoresis Methods 0.000 description 2
238000011534 incubation Methods 0.000 description 2
239000000411 inducer Substances 0.000 description 2
238000005259 measurement Methods 0.000 description 2
235000019319 peptone Nutrition 0.000 description 2
235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 2
229920000053 polysorbate 80 Polymers 0.000 description 2
239000000047 product Substances 0.000 description 2
108091008146 restriction endonucleases Proteins 0.000 description 2
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
239000000243 solution Substances 0.000 description 2
239000004474 valine Substances 0.000 description 2
239000012138 yeast extract Substances 0.000 description 2
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
DGYWXYFLXYIOCP-KBPBESRZSA-N (2s)-n-[2-[[(2s)-5-(diaminomethylideneamino)-1-(4-nitroanilino)-1-oxopentan-2-yl]amino]-2-oxoethyl]-5-oxopyrrolidine-2-carboxamide Chemical compound N([C@@H](CCCN=C(N)N)C(=O)NC=1C=CC(=CC=1)[N+]([O-])=O)C(=O)CNC(=O)[C@@H]1CCC(=O)N1 DGYWXYFLXYIOCP-KBPBESRZSA-N 0.000 description 1
ZORQXIQZAOLNGE-UHFFFAOYSA-N 1,1-difluorocyclohexane Chemical compound FC1(F)CCCCC1 ZORQXIQZAOLNGE-UHFFFAOYSA-N 0.000 description 1
SXOUIMVOMIGLHO-UHFFFAOYSA-N 3-(1h-indol-2-yl)prop-2-enoic acid Chemical compound C1=CC=C2NC(C=CC(=O)O)=CC2=C1 SXOUIMVOMIGLHO-UHFFFAOYSA-N 0.000 description 1
229920001817 Agar Polymers 0.000 description 1
GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
239000005695 Ammonium acetate Substances 0.000 description 1
108010039627 Aprotinin Proteins 0.000 description 1
208000031104 Arterial Occlusive disease Diseases 0.000 description 1
235000014469 Bacillus subtilis Nutrition 0.000 description 1
102000053602 DNA Human genes 0.000 description 1
241000588914 Enterobacter Species 0.000 description 1
108010053070 Glutathione Disulfide Proteins 0.000 description 1
XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
239000004472 Lysine Substances 0.000 description 1
108091005804 Peptidases Proteins 0.000 description 1
102000035195 Peptidases Human genes 0.000 description 1
102000013566 Plasminogen Human genes 0.000 description 1
108010051456 Plasminogen Proteins 0.000 description 1
229920003171 Poly (ethylene oxide) Polymers 0.000 description 1
241000589516 Pseudomonas Species 0.000 description 1
208000010378 Pulmonary Embolism Diseases 0.000 description 1
241000607142 Salmonella Species 0.000 description 1
241000607720 Serratia Species 0.000 description 1
229930006000 Sucrose Natural products 0.000 description 1
CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
206010053648 Vascular occlusion Diseases 0.000 description 1
239000008272 agar Substances 0.000 description 1
235000019257 ammonium acetate Nutrition 0.000 description 1
229940043376 ammonium acetate Drugs 0.000 description 1
BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
229910052921 ammonium sulfate Inorganic materials 0.000 description 1
235000011130 ammonium sulphate Nutrition 0.000 description 1
150000001450 anions Chemical class 0.000 description 1
238000000137 annealing Methods 0.000 description 1
229960004405 aprotinin Drugs 0.000 description 1
WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
238000009835 boiling Methods 0.000 description 1
210000004899 c-terminal region Anatomy 0.000 description 1
239000005018 casein Substances 0.000 description 1
BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
235000021240 caseins Nutrition 0.000 description 1
238000005119 centrifugation Methods 0.000 description 1
239000003638 chemical reducing agent Substances 0.000 description 1
230000000295 complement effect Effects 0.000 description 1
239000002299 complementary DNA Substances 0.000 description 1
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
235000018417 cysteine Nutrition 0.000 description 1
239000005549 deoxyribonucleoside 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
238000005516 engineering process Methods 0.000 description 1
230000002255 enzymatic effect Effects 0.000 description 1
238000011156 evaluation Methods 0.000 description 1
238000000605 extraction Methods 0.000 description 1
239000003527 fibrinolytic agent Substances 0.000 description 1
238000004108 freeze drying Methods 0.000 description 1
238000002523 gelfiltration Methods 0.000 description 1
229960003180 glutathione Drugs 0.000 description 1
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 1
239000001963 growth medium Substances 0.000 description 1
229960000789 guanidine hydrochloride Drugs 0.000 description 1
238000010438 heat treatment Methods 0.000 description 1
238000004128 high performance liquid chromatography Methods 0.000 description 1
230000001939 inductive effect Effects 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
230000000977 initiatory effect Effects 0.000 description 1
238000009434 installation Methods 0.000 description 1
238000002955 isolation Methods 0.000 description 1
AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
229960000310 isoleucine Drugs 0.000 description 1
239000008101 lactose Substances 0.000 description 1
229910052943 magnesium sulfate Inorganic materials 0.000 description 1
235000019341 magnesium sulphate Nutrition 0.000 description 1
235000013372 meat Nutrition 0.000 description 1
108020004999 messenger RNA Proteins 0.000 description 1
DEQXHPXOGUSHDX-UHFFFAOYSA-N methylaminomethanetriol;hydrochloride Chemical compound Cl.CNC(O)(O)O DEQXHPXOGUSHDX-UHFFFAOYSA-N 0.000 description 1
239000000203 mixture Substances 0.000 description 1
208000010125 myocardial infarction Diseases 0.000 description 1
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 1
239000008188 pellet Substances 0.000 description 1
239000008363 phosphate buffer Substances 0.000 description 1
150000008300 phosphoramidites Chemical class 0.000 description 1
230000000865 phosphorylative effect Effects 0.000 description 1
229920002401 polyacrylamide Polymers 0.000 description 1
238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
229920001184 polypeptide Polymers 0.000 description 1
108090000765 processed proteins & peptides Proteins 0.000 description 1
102000004196 processed proteins & peptides Human genes 0.000 description 1
235000019260 propionic acid Nutrition 0.000 description 1
IUVKMZGDUIUOCP-BTNSXGMBSA-N quinbolone Chemical compound O([C@H]1CC[C@H]2[C@H]3[C@@H]([C@]4(C=CC(=O)C=C4CC3)C)CC[C@@]21C)C1=CCCC1 IUVKMZGDUIUOCP-BTNSXGMBSA-N 0.000 description 1
239000011541 reaction mixture Substances 0.000 description 1
238000004007 reversed phase HPLC Methods 0.000 description 1
239000012266 salt solution Substances 0.000 description 1
229960002055 saruplase Drugs 0.000 description 1
229920006395 saturated elastomer Polymers 0.000 description 1
238000000926 separation method Methods 0.000 description 1
238000010532 solid phase synthesis reaction Methods 0.000 description 1
239000001593 sorbitan monooleate Substances 0.000 description 1
235000011069 sorbitan monooleate Nutrition 0.000 description 1
229940035049 sorbitan monooleate Drugs 0.000 description 1
238000010186 staining Methods 0.000 description 1
239000005720 sucrose Substances 0.000 description 1
239000010414 supernatant solution Substances 0.000 description 1
239000012085 test solution Substances 0.000 description 1
230000001225 therapeutic effect Effects 0.000 description 1
238000002560 therapeutic procedure Methods 0.000 description 1
230000005030 transcription termination Effects 0.000 description 1
238000012546 transfer Methods 0.000 description 1
125000002221 trityl group Chemical group [H]C1=C([H])C([H])=C([H])C([H])=C1C([*])(C1=C(C(=C(C(=C1[H])[H])[H])[H])[H])C1=C([H])C([H])=C([H])C([H])=C1[H] 0.000 description 1
238000011144 upstream manufacturing Methods 0.000 description 1
210000002700 urine Anatomy 0.000 description 1
208000021331 vascular occlusion disease Diseases 0.000 description 1
239000011800 void 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
- 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
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/67—General methods for enhancing the expression
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/70—Vectors or expression systems specially adapted for E. coli
- 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

Health & Medical Sciences (AREA)
Genetics & Genomics (AREA)
Life Sciences & Earth Sciences (AREA)
Engineering & Computer Science (AREA)
Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Wood Science & Technology (AREA)
Bioinformatics & Cheminformatics (AREA)
Zoology (AREA)
Biomedical Technology (AREA)
General Engineering & Computer Science (AREA)
Biotechnology (AREA)
Biochemistry (AREA)
General Health & Medical Sciences (AREA)
Molecular Biology (AREA)
Microbiology (AREA)
Physics & Mathematics (AREA)
Biophysics (AREA)
Plant Pathology (AREA)
Medicinal Chemistry (AREA)
Enzymes And Modification Thereof (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Saccharide Compounds (AREA)
Peptides Or Proteins (AREA)

DD90342894A 1989-07-19 1990-07-18 Verfahren zur herstellung von neuen plasmiden und deren verwendung bei der gewinnung eines plasminogenaktivators DD298426A5 (de)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
DE3923866		1989-07-19

Publications (1)

Publication Number	Publication Date
DD298426A5 true DD298426A5 (de)	1992-02-20

Family

ID=6385369

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
DD90342894A DD298426A5 (de)	1989-07-19	1990-07-18	Verfahren zur herstellung von neuen plasmiden und deren verwendung bei der gewinnung eines plasminogenaktivators

Country Status (29)

Country	Link
US (1)	US5637503A (fr)
EP (1)	EP0408945B1 (fr)
JP (1)	JP3236284B2 (fr)
KR (1)	KR0167761B1 (fr)
AT (1)	ATE131534T1 (fr)
AU (1)	AU631662B2 (fr)
CA (1)	CA2020656C (fr)
DD (1)	DD298426A5 (fr)
DE (2)	DE4020438A1 (fr)
DK (1)	DK0408945T3 (fr)
ES (1)	ES2083399T3 (fr)
FI (1)	FI102386B (fr)
GR (1)	GR3019294T3 (fr)
HR (1)	HRP920596B1 (fr)
HU (1)	HU214243B (fr)
IE (1)	IE901849A1 (fr)
IL (1)	IL94529A (fr)
LT (1)	LT3611B (fr)
LV (1)	LV10120B (fr)
MT (1)	MTP1063B (fr)
NO (1)	NO304952B1 (fr)
NZ (1)	NZ234542A (fr)
PL (1)	PL166199B1 (fr)
PT (1)	PT94776B (fr)
RU (1)	RU2073720C1 (fr)
SI (1)	SI9011347B (fr)
SK (1)	SK306790A3 (fr)
YU (1)	YU48371B (fr)
ZA (1)	ZA904006B (fr)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US3777528A (en) *	1969-11-27	1973-12-11	Cefilac	Method of hot piercing metal billets

Families Citing this family (12)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
DE4101736A1 (de) *	1991-01-22	1992-07-23	Gruenenthal Gmbh	Neue als plasminogenaktivatoren einsetzbare polypeptide, dafuer codierende plasmide und verfahren zu deren herstellung und deren verwendung
DE4440892A1 (de) *	1994-11-17	1996-05-23	Gruenenthal Gmbh	Proteine mit fibrinolytischen und gerinnungshemmenden Eigenschaften
DE4442665A1 (de) *	1994-11-30	1996-06-05	Gruenenthal Gmbh	Chimäre Proteine mit fibrinolytischen und thrombinhemmenden Eigenschaften
KR100467034B1 (ko) *	1996-12-27	2006-04-07	주식회사 엘지생활건강	압축성형타입오일케익화장료및그의제조방법
KR100372233B1 (ko) *	1997-03-12	2003-06-11	주식회사 코리아나화장품	미백 파우더, 그의 제조방법 및 그를 함유하는 메이크업 미백 화장료
RU2140453C1 (ru) *	1999-04-06	1999-10-27	Общество с ограниченной ответственностью Научно-производственное предприятие "Техноген"	Рекомбинантная плазмидная днк p ua bc22, кодирующая модифицированный активатор плазминогена урокиназного типа, нетранслируемый днк-элемент - искусственная межгенная последовательность мгп14 и штамм бактерий escherichia coli - продуцент модифицированного активатора плазминогена урокиназного типа
KR100341638B1 (ko) *	2000-03-17	2002-06-22	유상옥,송운한	기능성 표면처리 분체의 제조 방법 및 이를 함유하는메이크업 화장료 조성물
JP4124639B2 (ja) *	2002-12-17	2008-07-23	株式会社日本触媒	大腸菌を用いたｓ−ヒドロキシニトリルリアーゼの製造方法
US7906276B2 (en) *	2004-06-30	2011-03-15	Kimberly-Clark Worldwide, Inc.	Enzymatic detection techniques
AU2007352618B2 (en)	2007-05-02	2013-07-18	Boehringer Ingelheim Animal Health USA Inc.	DNA plasmids having improved expression and stability
RU2553533C2 (ru) *	2013-10-23	2015-06-20	Общество с ограниченной ответственностью "Международный биотехнологический центр "Генериум" ("МБЦ "Генериум")	Способ выделения и очистки рекомбинантной человеческой проурокиназы м5
CN104555732A (zh) *	2015-01-18	2015-04-29	河南省中原起重机械总厂	一种多功能门式起重机

Family Cites Families (9)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4370417A (en) *	1980-04-03	1983-01-25	Abbott Laboratories	Recombinant deoxyribonucleic acid which codes for plasminogen activator
US4558010A (en) *	1980-04-03	1985-12-10	Abbott Laboratories	Recombinant deoxyribonucleic acid which codes for plasminogen activator and method of making plasminogen activator protein therefrom
FI88932C (fi) *	1982-04-15	1993-07-26	Genentech Inc	Framstaellning av funktionellt maenskligt urokinasprotein
US4710464A (en) *	1984-09-27	1987-12-01	Eli Lilly And Company	Transcription terminators
AU5390286A (en) *	1985-01-25	1986-08-13	Sagami Chemical Research Center	Stabilized human prourokinase
FR2594845B1 (fr) *	1986-02-21	1989-12-01	Genetica	Preparation par voie microbiologique de l'activateur tissulaire humain du plasminogene (t-pa) et conversion de l'enzyme ainsi obtenue en sa forme active
FI100106B (fi) *	1986-12-05	1997-09-30	Novartis Ag	Menetelmä plasminogeenin yksisäikeisen yhdistelmäaktivaattorin valmist amiseksi
IL86801A0 (en) *	1987-08-10	1988-11-30	Lepetit Spa	Method for preparing single chain urokinase
WO1989003886A1 (fr) *	1987-10-30	1989-05-05	Oncogen, A Limited Partnership	Systemes d'expression destines a la preparation de polypeptides dans des cellules procaryotiques

1990
- 1990-05-22 IE IE184990A patent/IE901849A1/en not_active Application Discontinuation
- 1990-05-23 ZA ZA904006A patent/ZA904006B/xx unknown
- 1990-05-28 IL IL94529A patent/IL94529A/xx not_active IP Right Cessation
- 1990-06-19 NO NO902720A patent/NO304952B1/no not_active IP Right Cessation
- 1990-06-20 SK SK3067-90A patent/SK306790A3/sk unknown
- 1990-06-25 HU HU903970A patent/HU214243B/hu not_active IP Right Cessation
- 1990-06-27 DE DE4020438A patent/DE4020438A1/de not_active Withdrawn
- 1990-06-28 MT MT1063A patent/MTP1063B/xx unknown
- 1990-06-29 EP EP90112400A patent/EP0408945B1/fr not_active Expired - Lifetime
- 1990-06-29 AT AT90112400T patent/ATE131534T1/de not_active IP Right Cessation
- 1990-06-29 ES ES90112400T patent/ES2083399T3/es not_active Expired - Lifetime
- 1990-06-29 DK DK90112400.8T patent/DK0408945T3/da active
- 1990-06-29 DE DE59009961T patent/DE59009961D1/de not_active Expired - Fee Related
- 1990-07-06 CA CA002020656A patent/CA2020656C/fr not_active Expired - Fee Related
- 1990-07-09 AU AU58832/90A patent/AU631662B2/en not_active Ceased
- 1990-07-11 SI SI9011347A patent/SI9011347B/sl unknown
- 1990-07-11 YU YU134790A patent/YU48371B/sh unknown
- 1990-07-12 US US07/551,907 patent/US5637503A/en not_active Expired - Fee Related
- 1990-07-17 NZ NZ234542A patent/NZ234542A/xx unknown
- 1990-07-17 PL PL90286087A patent/PL166199B1/pl unknown
- 1990-07-18 RU SU4831114/13A patent/RU2073720C1/ru not_active IP Right Cessation
- 1990-07-18 JP JP18816990A patent/JP3236284B2/ja not_active Expired - Fee Related
- 1990-07-18 KR KR1019900010860A patent/KR0167761B1/ko not_active Expired - Fee Related
- 1990-07-18 FI FI903640A patent/FI102386B/fi not_active IP Right Cessation
- 1990-07-18 DD DD90342894A patent/DD298426A5/de not_active IP Right Cessation
- 1990-07-19 PT PT94776A patent/PT94776B/pt not_active IP Right Cessation
1992
- 1992-09-29 HR HRP-1347/90A patent/HRP920596B1/xx not_active IP Right Cessation
- 1992-11-13 LV LVP-92-204A patent/LV10120B/lv unknown
1993
- 1993-07-12 LT LTIP776A patent/LT3611B/lt not_active IP Right Cessation
1996
- 1996-03-13 GR GR960400698T patent/GR3019294T3/el unknown

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US3777528A (en) *	1969-11-27	1973-12-11	Cefilac	Method of hot piercing metal billets

Also Published As

Publication number	Publication date
HRP920596B1 (en)	1999-12-31
HUT54211A (en)	1991-01-28
HU214243B (hu)	1998-03-02
AU631662B2 (en)	1992-12-03
AU5883290A (en)	1991-01-24
IL94529A0 (en)	1991-03-10
KR910003105A (ko)	1991-02-26
PT94776B (pt)	1997-09-30
KR0167761B1 (ko)	1999-01-15
FI903640A0 (fi)	1990-07-18
EP0408945B1 (fr)	1995-12-13
CA2020656A1 (fr)	1991-01-20
US5637503A (en)	1997-06-10
MTP1063B (en)	1991-04-08
FI102386B1 (fi)	1998-11-30
RU2073720C1 (ru)	1997-02-20
ES2083399T3 (es)	1996-04-16
DK0408945T3 (da)	1996-04-09
LV10120A (lv)	1994-05-10
JP3236284B2 (ja)	2001-12-10
HK1005193A1 (en)	1998-12-24
SI9011347B (sl)	1999-02-28
NO902720D0 (no)	1990-06-19
PL286087A1 (en)	1991-03-11
NZ234542A (en)	1991-09-25
EP0408945A1 (fr)	1991-01-23
HRP920596A2 (en)	1998-06-30
HU903970D0 (en)	1990-11-28
GR3019294T3 (en)	1996-06-30
SK280028B6 (sk)	1999-07-12
IL94529A (en)	1997-11-20
LV10120B (en)	1994-10-20
IE901849A1 (en)	1991-06-19
YU134790A (sh)	1992-12-21
JPH0365189A (ja)	1991-03-20
YU48371B (sh)	1998-07-10
ATE131534T1 (de)	1995-12-15
ZA904006B (en)	1991-03-27
PL166199B1 (pl)	1995-04-28
NO304952B1 (no)	1999-03-08
CA2020656C (fr)	2001-05-22
DE59009961D1 (de)	1996-01-25
DE4020438A1 (de)	1991-01-31
PT94776A (pt)	1991-03-20
SI9011347A (sl)	1998-04-30
FI102386B (fi)	1998-11-30
LT3611B (en)	1995-12-27
LTIP776A (en)	1995-01-31
SK306790A3 (en)	1999-07-12
NO902720L (no)	1991-01-21

Legal Events

Date	Code	Title	Description
1999-02-04	ENJ	Ceased due to non-payment of renewal fee

Publication	Publication Date	Title
DE3786767T3 (de)	1998-04-16	Neues Polypeptid.
DE69018920T2 (de)	1995-09-07	Verwendung von dns-fragmenten, die ein signalpeptid kodieren zur sekretion von reifen proteinen in rekombinanten hefen, expressions-kassetten, transformierte hefen und verfahren zur herstellung dieser proteine.
DE3881776T2 (de)	1993-11-18	DNS-Konstruktionen, enthaltend eine Kluyveromyces-alpha-Factor-Leadersequenz zur Leitung der Sekretion von heterologen Polypeptiden.
DE3382760T2 (de)	1995-03-02	Herstellung von funktionellen menschlichen Urokinasepolypeptiden.
DE3751128T2 (de)	1995-07-20	Rekombinante gereinigte Protease, Nexin.
DE3316297C2 (fr)	1989-09-21
DE3785864T2 (de)	1994-01-20	Verfahren zur Herstellung von menschlichem Epidermalwachstumsfaktor und dessen Analogen.
DE69012888T2 (de)	1995-06-01	Plasminogenaktivator.
DE3687651T2 (de)	1993-06-24	Analoge des gewebespezifischen plasminogenaktivators.
EP0448093B1 (fr)	1996-03-06	Sécrétion des dérivés de hirudine
EP0408945B1 (fr)	1995-12-13	Plasmides, leur préparation et leur utilisation pour obtenir un activateur de plasminogène
DD258026A5 (de)	1988-07-06	Verfahren zur Herstellung von Human-Gewebeplasminogen-Aktivator-Mutanten
DE3587875T2 (de)	1994-10-13	Rekombinantverfahren zur herstellung von serinproteaseinhibitoren, sowie dns-sequenzen dazu.
DE3537176C2 (de)	1994-06-09	Gewebeplasminogenaktivator und Verfahren zu seiner Herstellung
DE3643158A1 (de)	1987-11-19	Gewebs-plasminogen-aktivator(tpa) - derivat und seine herstellung
DE3752008T2 (de)	1997-08-14	Hybride Plasminogenaktivatoren
DE69010096T2 (de)	1994-10-13	Expression und Sekretion von reifem menschlichem beta-Interleukin-1 in Bacillus subtilis und Mittel und Verfahren zu deren Ausführung.
DE3879823T2 (de)	1993-07-08	Verfahren zur herstellung von menschlichem wachstumshormon.
DE68918279T2 (de)	1995-03-23	Plasminogenaktivator-varianten und verfahren zu ihrer herstellung.
EP0496327B1 (fr)	2001-08-16	Procédé pour la préparation de polypeptides ayant l'activité de la prourokinase
DD274053A5 (de)	1989-12-06	Verfahren zur Produktion eines menschlichen, einkettigen Plasminogenaktivators
DE68922859T2 (de)	1995-09-21	Trombolytischer wirkstoff mit modifikation der domäne der kringle.
EP0244627A2 (fr)	1987-11-11	Vecteurs d'expression pour la production de polypeptides
DE3853479T2 (de)	1995-09-28	Ausgeglichenes, konstitutives, induzierbares transkriptionssystem.
DE3877197T2 (de)	1993-04-29	Verfahren zur herstellung von hirudin.

DD298426A5 - Verfahren zur herstellung von neuen plasmiden und deren verwendung bei der gewinnung eines plasminogenaktivators - Google Patents

Info

Links

Classifications

Landscapes

Applications Claiming Priority (1)

Publications (1)

Family

ID=6385369

Family Applications (1)

Country Status (29)

Cited By (1)

Families Citing this family (12)

Family Cites Families (9)

Cited By (1)

Also Published As

Similar Documents

Legal Events