UA75102C2 - METHODS FOR THE MASS PRODUCTION OF A RECOMBINANT DNA-DERIVED MOLECULES OF tPA OR K2S - Google Patents

METHODS FOR THE MASS PRODUCTION OF A RECOMBINANT DNA-DERIVED MOLECULES OF tPA OR K2S Download PDF

Info

Publication number: UA75102C2
Authority: UA; Ukraine
Prior art keywords: variant; ira; molecule; dna; vector
Prior art date: 2000-11-14

Application number

UA2003065487A

Other languages

English (en)

Ukrainian (uk)

Original Assignee

Boehringer Ingelheim Int

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.)

2000-11-14

Filing date

2001-07-11

Publication date

2006-03-15

2001-07-11 Application filed by Boehringer Ingelheim Int filed Critical Boehringer Ingelheim Int

2006-03-15 Publication of UA75102C2 publication Critical patent/UA75102C2/uk

Links

238000000034 method Methods 0.000 title claims abstract description 66
238000004519 manufacturing process Methods 0.000 title abstract description 7
108020004414 DNA Proteins 0.000 claims abstract description 59
239000013598 vector Substances 0.000 claims abstract description 51
108090000623 proteins and genes Proteins 0.000 claims abstract description 47
102000004169 proteins and genes Human genes 0.000 claims abstract description 37
102000003978 Tissue Plasminogen Activator Human genes 0.000 claims abstract description 21
108090000373 Tissue Plasminogen Activator Proteins 0.000 claims abstract description 21
108010076504 Protein Sorting Signals Proteins 0.000 claims abstract description 19
210000001236 prokaryotic cell Anatomy 0.000 claims abstract description 16
229960000187 tissue plasminogen activator Drugs 0.000 claims abstract description 14
108020004511 Recombinant DNA Proteins 0.000 claims abstract description 13
150000001413 amino acids Chemical class 0.000 claims description 53
108091028043 Nucleic acid sequence Proteins 0.000 claims description 21
102000012479 Serine Proteases Human genes 0.000 claims description 17
108010022999 Serine Proteases Proteins 0.000 claims description 17
102000039446 nucleic acids Human genes 0.000 claims description 10
108020004707 nucleic acids Proteins 0.000 claims description 10
108020004705 Codon Proteins 0.000 claims description 9
150000007523 nucleic acids Chemical class 0.000 claims description 9
239000002773 nucleotide Substances 0.000 claims description 8
125000003729 nucleotide group Chemical group 0.000 claims description 8
108090000765 processed proteins & peptides Proteins 0.000 claims description 8
238000013518 transcription Methods 0.000 claims description 8
230000035897 transcription Effects 0.000 claims description 8
238000011144 upstream manufacturing Methods 0.000 claims description 2
MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 abstract description 2
230000002537 thrombolytic effect Effects 0.000 abstract description 2
108010079246 OMPA outer membrane proteins Proteins 0.000 abstract 1
239000012634 fragment Substances 0.000 description 19
235000010469 Glycine max Nutrition 0.000 description 18
239000000047 product Substances 0.000 description 18
102000053602 DNA Human genes 0.000 description 17
239000012228 culture supernatant Substances 0.000 description 15
102000037865 fusion proteins Human genes 0.000 description 13
108020001507 fusion proteins Proteins 0.000 description 13
125000003275 alpha amino acid group Chemical group 0.000 description 12
239000000499 gel Substances 0.000 description 12
230000014509 gene expression Effects 0.000 description 12
239000000126 substance Substances 0.000 description 12
241001494479 Pecora Species 0.000 description 11
102000013566 Plasminogen Human genes 0.000 description 11
108010051456 Plasminogen Proteins 0.000 description 11
210000004027 cell Anatomy 0.000 description 11
244000068988 Glycine max Species 0.000 description 10
108010001336 Horseradish Peroxidase Proteins 0.000 description 10
230000000694 effects Effects 0.000 description 10
230000002255 enzymatic effect Effects 0.000 description 10
230000003321 amplification Effects 0.000 description 8
238000003776 cleavage reaction Methods 0.000 description 8
239000012528 membrane Substances 0.000 description 8
239000000203 mixture Substances 0.000 description 8
238000003199 nucleic acid amplification method Methods 0.000 description 8
230000007017 scission Effects 0.000 description 8
102000035195 Peptidases Human genes 0.000 description 7
108091005804 Peptidases Proteins 0.000 description 7
239000004365 Protease Substances 0.000 description 7
230000015572 biosynthetic process Effects 0.000 description 7
238000001962 electrophoresis Methods 0.000 description 7
230000004048 modification Effects 0.000 description 7
238000012986 modification Methods 0.000 description 7
230000035772 mutation Effects 0.000 description 7
230000008569 process Effects 0.000 description 7
230000028327 secretion Effects 0.000 description 7
238000006243 chemical reaction Methods 0.000 description 6
201000001441 melanoma Diseases 0.000 description 6
210000001322 periplasm Anatomy 0.000 description 6
238000010521 absorption reaction Methods 0.000 description 5
239000002245 particle Substances 0.000 description 5
229920002401 polyacrylamide Polymers 0.000 description 5
238000012546 transfer Methods 0.000 description 5
241000894006 Bacteria Species 0.000 description 4
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
102000008946 Fibrinogen Human genes 0.000 description 4
108010049003 Fibrinogen Proteins 0.000 description 4
241000700605 Viruses Species 0.000 description 4
229960000723 ampicillin Drugs 0.000 description 4
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 4
238000004458 analytical method Methods 0.000 description 4
230000001580 bacterial effect Effects 0.000 description 4
238000010367 cloning Methods 0.000 description 4
238000010276 construction Methods 0.000 description 4
229950003499 fibrin Drugs 0.000 description 4
229940012952 fibrinogen Drugs 0.000 description 4
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 4
239000011159 matrix material Substances 0.000 description 4
239000000546 pharmaceutical excipient Substances 0.000 description 4
239000013612 plasmid Substances 0.000 description 4
229920001184 polypeptide Polymers 0.000 description 4
238000002360 preparation method Methods 0.000 description 4
102000004196 processed proteins & peptides Human genes 0.000 description 4
230000000644 propagated effect Effects 0.000 description 4
239000000523 sample Substances 0.000 description 4
239000000243 solution Substances 0.000 description 4
230000009466 transformation Effects 0.000 description 4
108010010803 Gelatin Proteins 0.000 description 3
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 description 3
239000000020 Nitrocellulose Substances 0.000 description 3
239000004098 Tetracycline Substances 0.000 description 3
239000011543 agarose gel Substances 0.000 description 3
230000003024 amidolytic effect Effects 0.000 description 3
230000001086 cytosolic effect Effects 0.000 description 3
238000001514 detection method Methods 0.000 description 3
239000008273 gelatin Substances 0.000 description 3
229920000159 gelatin Polymers 0.000 description 3
235000019322 gelatine Nutrition 0.000 description 3
235000011852 gelatine desserts Nutrition 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
238000011534 incubation Methods 0.000 description 3
230000003834 intracellular effect Effects 0.000 description 3
238000011031 large-scale manufacturing process Methods 0.000 description 3
239000003550 marker Substances 0.000 description 3
229920001220 nitrocellulos Polymers 0.000 description 3
229940012957 plasmin Drugs 0.000 description 3
238000000746 purification Methods 0.000 description 3
108091008146 restriction endonucleases Proteins 0.000 description 3
238000002741 site-directed mutagenesis Methods 0.000 description 3
239000000758 substrate Substances 0.000 description 3
229960002180 tetracycline Drugs 0.000 description 3
229930101283 tetracycline Natural products 0.000 description 3
235000019364 tetracycline Nutrition 0.000 description 3
150000003522 tetracyclines Chemical class 0.000 description 3
238000005406 washing Methods 0.000 description 3
208000031104 Arterial Occlusive disease Diseases 0.000 description 2
CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
102000004190 Enzymes Human genes 0.000 description 2
108090000790 Enzymes Proteins 0.000 description 2
241000901143 Etia Species 0.000 description 2
108010024636 Glutathione Proteins 0.000 description 2
208000010378 Pulmonary Embolism Diseases 0.000 description 2
241000714474 Rous sarcoma virus Species 0.000 description 2
241000408490 Sovia Species 0.000 description 2
206010000891 acute myocardial infarction Diseases 0.000 description 2
BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
229910052921 ammonium sulfate Inorganic materials 0.000 description 2
235000011130 ammonium sulphate Nutrition 0.000 description 2
238000000137 annealing Methods 0.000 description 2
208000021328 arterial occlusion Diseases 0.000 description 2
210000001367 artery Anatomy 0.000 description 2
230000003115 biocidal effect Effects 0.000 description 2
230000008827 biological function Effects 0.000 description 2
125000004122 cyclic group Chemical group 0.000 description 2
210000000805 cytoplasm Anatomy 0.000 description 2
238000004925 denaturation Methods 0.000 description 2
230000036425 denaturation Effects 0.000 description 2
230000001419 dependent effect Effects 0.000 description 2
238000010586 diagram Methods 0.000 description 2
238000000502 dialysis Methods 0.000 description 2
239000003937 drug carrier Substances 0.000 description 2
229940088598 enzyme Drugs 0.000 description 2
239000003102 growth factor Substances 0.000 description 2
239000001963 growth medium Substances 0.000 description 2
238000003119 immunoblot Methods 0.000 description 2
230000001939 inductive effect Effects 0.000 description 2
210000004962 mammalian cell Anatomy 0.000 description 2
239000013642 negative control Substances 0.000 description 2
230000001590 oxidative effect Effects 0.000 description 2
230000002093 peripheral effect Effects 0.000 description 2
239000008194 pharmaceutical composition Substances 0.000 description 2
239000013641 positive control Substances 0.000 description 2
239000011541 reaction mixture Substances 0.000 description 2
238000006467 substitution reaction Methods 0.000 description 2
230000001225 therapeutic effect Effects 0.000 description 2
DIGQNXIGRZPYDK-WKSCXVIASA-N (2R)-6-amino-2-[[2-[[(2S)-2-[[2-[[(2R)-2-[[(2S)-2-[[(2R,3S)-2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S,3S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2R)-2-[[2-[[2-[[2-[(2-amino-1-hydroxyethylidene)amino]-3-carboxy-1-hydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1,5-dihydroxy-5-iminopentylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]hexanoic acid Chemical compound C[C@@H]([C@@H](C(=N[C@@H](CS)C(=N[C@@H](C)C(=N[C@@H](CO)C(=NCC(=N[C@@H](CCC(=N)O)C(=NC(CS)C(=N[C@H]([C@H](C)O)C(=N[C@H](CS)C(=N[C@H](CO)C(=NCC(=N[C@H](CS)C(=NCC(=N[C@H](CCCCN)C(=O)O)O)O)O)O)O)O)O)O)O)O)O)O)O)N=C([C@H](CS)N=C([C@H](CO)N=C([C@H](CO)N=C([C@H](C)N=C(CN=C([C@H](CO)N=C([C@H](CS)N=C(CN=C(C(CS)N=C(C(CC(=O)O)N=C(CN)O)O)O)O)O)O)O)O)O)O)O)O DIGQNXIGRZPYDK-WKSCXVIASA-N 0.000 description 1
VEPOHXYIFQMVHW-PVJVQHJQSA-N (2r,3r)-2,3-dihydroxybutanedioic acid;(2s,3s)-3,4-dimethyl-2-phenylmorpholine Chemical compound OC(=O)[C@H](O)[C@@H](O)C(O)=O.O1CCN(C)[C@@H](C)[C@@H]1C1=CC=CC=C1 VEPOHXYIFQMVHW-PVJVQHJQSA-N 0.000 description 1
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
TYMLOMAKGOJONV-UHFFFAOYSA-N 4-nitroaniline Chemical compound NC1=CC=C([N+]([O-])=O)C=C1 TYMLOMAKGOJONV-UHFFFAOYSA-N 0.000 description 1
229920001817 Agar Polymers 0.000 description 1
QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
241000212977 Andira Species 0.000 description 1
108090000668 Annexin A2 Proteins 0.000 description 1
241000283725 Bos Species 0.000 description 1
241000283690 Bos taurus Species 0.000 description 1
206010006187 Breast cancer Diseases 0.000 description 1
208000026310 Breast neoplasm Diseases 0.000 description 1
206010011086 Coronary artery occlusion Diseases 0.000 description 1
241000701022 Cytomegalovirus Species 0.000 description 1
238000001712 DNA sequencing Methods 0.000 description 1
102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
206010051055 Deep vein thrombosis Diseases 0.000 description 1
229920002307 Dextran Polymers 0.000 description 1
241000402754 Erythranthe moschata Species 0.000 description 1
241000701533 Escherichia virus T4 Species 0.000 description 1
241000724791 Filamentous phage Species 0.000 description 1
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 1
108010053070 Glutathione Disulfide Proteins 0.000 description 1
208000032843 Hemorrhage Diseases 0.000 description 1
241000701024 Human betaherpesvirus 5 Species 0.000 description 1
101150098499 III gene Proteins 0.000 description 1
108060003951 Immunoglobulin Proteins 0.000 description 1
102000004310 Ion Channels Human genes 0.000 description 1
-1 K25 nucleic acid Chemical class 0.000 description 1
102000003960 Ligases Human genes 0.000 description 1
108090000364 Ligases Proteins 0.000 description 1
102000004895 Lipoproteins Human genes 0.000 description 1
108090001030 Lipoproteins Proteins 0.000 description 1
102000003792 Metallothionein Human genes 0.000 description 1
108090000157 Metallothionein Proteins 0.000 description 1
238000012408 PCR amplification Methods 0.000 description 1
238000010222 PCR analysis Methods 0.000 description 1
101710190786 PI protein Proteins 0.000 description 1
108010090127 Periplasmic Proteins Proteins 0.000 description 1
206010035226 Plasma cell myeloma Diseases 0.000 description 1
108010015078 Pregnancy-Associated alpha 2-Macroglobulins Proteins 0.000 description 1
102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
208000035415 Reinfection Diseases 0.000 description 1
108010086019 Secretin Proteins 0.000 description 1
102100037505 Secretin Human genes 0.000 description 1
229920002684 Sepharose Polymers 0.000 description 1
241000700584 Simplexvirus Species 0.000 description 1
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
208000006011 Stroke Diseases 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
229930006000 Sucrose Natural products 0.000 description 1
208000001435 Thromboembolism Diseases 0.000 description 1
108091023045 Untranslated Region Proteins 0.000 description 1
241000700618 Vaccinia virus Species 0.000 description 1
206010047249 Venous thrombosis Diseases 0.000 description 1
238000002835 absorbance Methods 0.000 description 1
230000004913 activation Effects 0.000 description 1
238000001042 affinity chromatography Methods 0.000 description 1
239000008272 agar Substances 0.000 description 1
238000000246 agarose gel electrophoresis Methods 0.000 description 1
125000000539 amino acid group Chemical group 0.000 description 1
238000012870 ammonium sulfate precipitation Methods 0.000 description 1
230000000890 antigenic effect Effects 0.000 description 1
239000003963 antioxidant agent Substances 0.000 description 1
235000006708 antioxidants Nutrition 0.000 description 1
229960005070 ascorbic acid Drugs 0.000 description 1
235000010323 ascorbic acid Nutrition 0.000 description 1
239000011668 ascorbic acid Substances 0.000 description 1
230000008901 benefit Effects 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
208000034158 bleeding Diseases 0.000 description 1
230000000740 bleeding effect Effects 0.000 description 1
230000000903 blocking effect Effects 0.000 description 1
230000023555 blood coagulation Effects 0.000 description 1
239000000872 buffer Substances 0.000 description 1
239000007853 buffer solution Substances 0.000 description 1
210000004899 c-terminal region Anatomy 0.000 description 1
229940041514 candida albicans extract Drugs 0.000 description 1
150000001720 carbohydrates Chemical class 0.000 description 1
235000014633 carbohydrates Nutrition 0.000 description 1
230000003197 catalytic effect Effects 0.000 description 1
238000004113 cell culture Methods 0.000 description 1
230000006037 cell lysis Effects 0.000 description 1
210000001627 cerebral artery Anatomy 0.000 description 1
238000012512 characterization method Methods 0.000 description 1
239000002738 chelating agent Substances 0.000 description 1
239000003153 chemical reaction reagent Substances 0.000 description 1
239000003795 chemical substances by application Substances 0.000 description 1
210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
230000001332 colony forming effect Effects 0.000 description 1
150000001875 compounds Chemical class 0.000 description 1
239000012468 concentrated sample Substances 0.000 description 1
238000012790 confirmation Methods 0.000 description 1
238000011109 contamination Methods 0.000 description 1
238000007334 copolymerization reaction Methods 0.000 description 1
230000009089 cytolysis Effects 0.000 description 1
238000012217 deletion Methods 0.000 description 1
230000037430 deletion Effects 0.000 description 1
229910003460 diamond Inorganic materials 0.000 description 1
239000010432 diamond Substances 0.000 description 1
201000010099 disease Diseases 0.000 description 1
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
239000003623 enhancer Substances 0.000 description 1
230000002708 enhancing effect Effects 0.000 description 1
238000011156 evaluation Methods 0.000 description 1
239000013604 expression vector Substances 0.000 description 1
238000000605 extraction Methods 0.000 description 1
238000000855 fermentation Methods 0.000 description 1
230000004151 fermentation Effects 0.000 description 1
239000003527 fibrinolytic agent Substances 0.000 description 1
238000001914 filtration Methods 0.000 description 1
239000008103 glucose Substances 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
210000002837 heart atrium Anatomy 0.000 description 1
230000013632 homeostatic process Effects 0.000 description 1
229940106780 human fibrinogen Drugs 0.000 description 1
238000009396 hybridization Methods 0.000 description 1
230000008105 immune reaction Effects 0.000 description 1
210000000987 immune system Anatomy 0.000 description 1
238000003018 immunoassay Methods 0.000 description 1
102000018358 immunoglobulin Human genes 0.000 description 1
230000006872 improvement Effects 0.000 description 1
230000002779 inactivation Effects 0.000 description 1
239000000411 inducer Substances 0.000 description 1
238000009776 industrial production Methods 0.000 description 1
239000003999 initiator Substances 0.000 description 1
238000003780 insertion Methods 0.000 description 1
230000037431 insertion Effects 0.000 description 1
238000007917 intracranial administration Methods 0.000 description 1
238000010253 intravenous injection Methods 0.000 description 1
229930027917 kanamycin Natural products 0.000 description 1
229960000318 kanamycin Drugs 0.000 description 1
SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound 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 SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
229930182823 kanamycin A Natural products 0.000 description 1
239000007788 liquid Substances 0.000 description 1
230000004807 localization Effects 0.000 description 1
239000000463 material Substances 0.000 description 1
230000007246 mechanism Effects 0.000 description 1
229940126601 medicinal product Drugs 0.000 description 1
239000002609 medium Substances 0.000 description 1
244000005700 microbiome Species 0.000 description 1
229940126619 mouse monoclonal antibody Drugs 0.000 description 1
231100000219 mutagenic Toxicity 0.000 description 1
230000003505 mutagenic effect Effects 0.000 description 1
201000000050 myeloid neoplasm Diseases 0.000 description 1
208000010125 myocardial infarction Diseases 0.000 description 1
230000003287 optical effect Effects 0.000 description 1
230000002018 overexpression Effects 0.000 description 1
230000003647 oxidation Effects 0.000 description 1
238000007254 oxidation reaction Methods 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
238000012858 packaging process Methods 0.000 description 1
229940124531 pharmaceutical excipient Drugs 0.000 description 1
239000000825 pharmaceutical preparation Substances 0.000 description 1
238000013492 plasmid preparation Methods 0.000 description 1
238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
239000011148 porous material Substances 0.000 description 1
239000002244 precipitate Substances 0.000 description 1
KCXFHTAICRTXLI-UHFFFAOYSA-N propane-1-sulfonic acid Chemical compound CCCS(O)(=O)=O KCXFHTAICRTXLI-UHFFFAOYSA-N 0.000 description 1
238000001243 protein synthesis Methods 0.000 description 1
239000012264 purified product Substances 0.000 description 1
230000007420 reactivation Effects 0.000 description 1
230000001105 regulatory effect Effects 0.000 description 1
238000004153 renaturation Methods 0.000 description 1
238000011160 research Methods 0.000 description 1
229920006395 saturated elastomer Polymers 0.000 description 1
239000012047 saturated solution Substances 0.000 description 1
229960002101 secretin Drugs 0.000 description 1
OWMZNFCDEHGFEP-NFBCVYDUSA-N secretin human Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(N)=O)[C@@H](C)O)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)C1=CC=CC=C1 OWMZNFCDEHGFEP-NFBCVYDUSA-N 0.000 description 1
230000003248 secreting effect Effects 0.000 description 1
230000035945 sensitivity Effects 0.000 description 1
230000001953 sensory effect Effects 0.000 description 1
230000035939 shock Effects 0.000 description 1
235000020183 skimmed milk Nutrition 0.000 description 1
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
239000007790 solid phase Substances 0.000 description 1
238000005063 solubilization Methods 0.000 description 1
230000007928 solubilization Effects 0.000 description 1
230000007480 spreading Effects 0.000 description 1
238000003892 spreading Methods 0.000 description 1
239000003381 stabilizer Substances 0.000 description 1
238000010186 staining Methods 0.000 description 1
239000005720 sucrose Substances 0.000 description 1
239000006228 supernatant Substances 0.000 description 1
238000003786 synthesis reaction Methods 0.000 description 1
230000009885 systemic effect Effects 0.000 description 1
229960000103 thrombolytic agent Drugs 0.000 description 1
230000014616 translation Effects 0.000 description 1
239000012137 tryptone Substances 0.000 description 1
241000701161 unidentified adenovirus Species 0.000 description 1
241001515965 unidentified phage Species 0.000 description 1
239000013603 viral vector Substances 0.000 description 1
239000012138 yeast extract Substances 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- 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)
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
- 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
- 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
- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
- 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
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
- 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)
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Engineering & Computer Science (AREA)
Organic Chemistry (AREA)
Bioinformatics & Cheminformatics (AREA)
Wood Science & Technology (AREA)
Zoology (AREA)
Genetics & Genomics (AREA)
General Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Biochemistry (AREA)
Biomedical Technology (AREA)
General Engineering & Computer Science (AREA)
General Chemical & Material Sciences (AREA)
Molecular Biology (AREA)
Biotechnology (AREA)
Chemical Kinetics & Catalysis (AREA)
Microbiology (AREA)
Animal Behavior & Ethology (AREA)
Pharmacology & Pharmacy (AREA)
Public Health (AREA)
Veterinary Medicine (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Cardiology (AREA)
Heart & Thoracic Surgery (AREA)
Vascular Medicine (AREA)
Urology & Nephrology (AREA)
Pulmonology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Enzymes And Modification Thereof (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Peptides Or Proteins (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Inorganic Compounds Of Heavy Metals (AREA)

UA2003065487A 2000-11-14 2001-07-11 METHODS FOR THE MASS PRODUCTION OF A RECOMBINANT DNA-DERIVED MOLECULES OF tPA OR K2S UA75102C2 (en)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
GBGB0027779.8A GB0027779D0 (en)	2000-11-14	2000-11-14	Methods for large scale production of recombinant dna-derived tpa or k2s molecules
PCT/EP2001/012857 WO2002040650A2 (en)	2000-11-14	2001-11-07	Methods for large scale production of recombinant dna-derived tpa or k2s molecules

Publications (1)

Publication Number	Publication Date
UA75102C2 true UA75102C2 (en)	2006-03-15

Family

ID=9903153

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
UA2003065487A UA75102C2 (en)	2000-11-14	2001-07-11	METHODS FOR THE MASS PRODUCTION OF A RECOMBINANT DNA-DERIVED MOLECULES OF tPA OR K2S

Country Status (31)

Country	Link
EP (1)	EP1407030B1 (cs)
JP (1)	JP2004520018A (cs)
KR (1)	KR100856346B1 (cs)
CN (1)	CN100567495C (cs)
AR (1)	AR031334A1 (cs)
AT (1)	ATE504652T1 (cs)
AU (2)	AU2002221815B2 (cs)
BG (1)	BG66121B1 (cs)
BR (1)	BR0115344A (cs)
CA (1)	CA2428642C (cs)
CZ (1)	CZ20031657A3 (cs)
DE (1)	DE60144395D1 (cs)
EA (1)	EA005163B1 (cs)
EC (1)	ECSP034573A (cs)
EE (1)	EE200300232A (cs)
GB (1)	GB0027779D0 (cs)
HR (1)	HRP20030377A2 (cs)
HU (1)	HUP0301619A3 (cs)
IL (2)	IL155568A0 (cs)
MX (1)	MXPA03004161A (cs)
MY (1)	MY129838A (cs)
NO (1)	NO20032143L (cs)
NZ (1)	NZ526280A (cs)
PL (1)	PL206783B1 (cs)
SK (1)	SK5792003A3 (cs)
TW (1)	TWI292782B (cs)
UA (1)	UA75102C2 (cs)
UY (1)	UY27020A1 (cs)
WO (1)	WO2002040650A2 (cs)
YU (1)	YU36103A (cs)
ZA (1)	ZA200303547B (cs)

Families Citing this family (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US6955910B2 (en)	2000-11-14	2005-10-18	Boehringer Ingelheim International Gmbh	Method for large scale production of recombinant DNA-derived TPA or K2S molecules
US7087412B2 (en)	2000-11-14	2006-08-08	Boehringer Ingelheim International Gmbh	Methods for large scale protein production in prokaryotes
IL190184A0 (en) *	2008-03-16	2009-02-11	Hadasit Med Res Service	tPA MUTANT IN THE TREATMENT OF ACUTE BRAIN INJURY AND NEURODEGENERATIVE DISORDERS

Family Cites Families (7)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
IL87276A (en) *	1987-08-03	1995-07-31	Fujisawa Pharmaceutical Co	Analog of tissue plasminogen activator comprising only the kringle 2 and protease domain dna encoding the same processes for the preparation thereof and pharmaceutical compositions containing the same
AU2660397A (en) *	1996-04-05	1997-10-29	Board Of Regents, The University Of Texas System	Methods for producing soluble, biologically-active disulfide bond-containing eukaryotic proteins in bacterial cells
US20020061576A1 (en) *	1997-05-28	2002-05-23	Paul A. Moore	Tissue plasminogen activator-like protease
US6083715A (en) *	1997-06-09	2000-07-04	Board Of Regents, The University Of Texas System	Methods for producing heterologous disulfide bond-containing polypeptides in bacterial cells
EP1048732A1 (de) *	1999-04-26	2000-11-02	F. Hoffmann-La Roche Ag	Verfahren zur Herstellung von natürlich gefalteten und sekretierten Proteinen
EP1077263A1 (de) *	1999-07-29	2001-02-21	F.Hoffmann-La Roche Ag	Verfahren zur Herstellung von natürlich gefalteten und sekretierten Proteinen durch Co-Sekretion von Chaperonen
GB0027782D0 (en) *	2000-11-14	2000-12-27	Boehringer Ingelheim Int	Methods fro large scale protein productio in prokaryotes

2000
- 2000-11-14 GB GBGB0027779.8A patent/GB0027779D0/en not_active Ceased
2001
- 2001-07-11 UA UA2003065487A patent/UA75102C2/uk unknown
- 2001-11-07 JP JP2002543647A patent/JP2004520018A/ja active Pending
- 2001-11-07 YU YU36103A patent/YU36103A/sh unknown
- 2001-11-07 EA EA200300502A patent/EA005163B1/ru not_active IP Right Cessation
- 2001-11-07 KR KR1020037006567A patent/KR100856346B1/ko not_active Expired - Fee Related
- 2001-11-07 DE DE60144395T patent/DE60144395D1/de not_active Expired - Lifetime
- 2001-11-07 MX MXPA03004161A patent/MXPA03004161A/es active IP Right Grant
- 2001-11-07 CN CNB018188982A patent/CN100567495C/zh not_active Expired - Fee Related
- 2001-11-07 WO PCT/EP2001/012857 patent/WO2002040650A2/en not_active Ceased
- 2001-11-07 HR HR20030377A patent/HRP20030377A2/hr not_active Application Discontinuation
- 2001-11-07 EP EP01996596A patent/EP1407030B1/en not_active Expired - Lifetime
- 2001-11-07 CZ CZ20031657A patent/CZ20031657A3/cs unknown
- 2001-11-07 PL PL361881A patent/PL206783B1/pl not_active IP Right Cessation
- 2001-11-07 AU AU2002221815A patent/AU2002221815B2/en not_active Ceased
- 2001-11-07 NZ NZ526280A patent/NZ526280A/en unknown
- 2001-11-07 BR BR0115344-7A patent/BR0115344A/pt not_active IP Right Cessation
- 2001-11-07 CA CA2428642A patent/CA2428642C/en not_active Expired - Fee Related
- 2001-11-07 HU HU0301619A patent/HUP0301619A3/hu unknown
- 2001-11-07 AU AU2181502A patent/AU2181502A/xx active Pending
- 2001-11-07 AT AT01996596T patent/ATE504652T1/de not_active IP Right Cessation
- 2001-11-07 EE EEP200300232A patent/EE200300232A/xx unknown
- 2001-11-07 IL IL15556801A patent/IL155568A0/xx unknown
- 2001-11-07 SK SK579-2003A patent/SK5792003A3/sk unknown
- 2001-11-12 MY MYPI20015201A patent/MY129838A/en unknown
- 2001-11-12 UY UY27020A patent/UY27020A1/es not_active Application Discontinuation
- 2001-11-13 TW TW090128128A patent/TWI292782B/zh not_active IP Right Cessation
- 2001-11-14 AR ARP010105298A patent/AR031334A1/es unknown
2003
- 2003-04-24 IL IL155568A patent/IL155568A/en not_active IP Right Cessation
- 2003-04-29 EC EC2003004573A patent/ECSP034573A/es unknown
- 2003-05-08 ZA ZA200303547A patent/ZA200303547B/en unknown
- 2003-05-08 BG BG107780A patent/BG66121B1/bg unknown
- 2003-05-13 NO NO20032143A patent/NO20032143L/no not_active Application Discontinuation

Also Published As

Publication number	Publication date
CN100567495C (zh)	2009-12-09
AU2181502A (en)	2002-05-27
BG66121B1 (bg)	2011-05-31
TWI292782B (en)	2008-01-21
IL155568A0 (en)	2003-11-23
HUP0301619A3 (en)	2006-11-28
AU2002221815B2 (en)	2007-08-23
MXPA03004161A (es)	2004-04-20
NO20032143D0 (no)	2003-05-13
WO2002040650A2 (en)	2002-05-23
MY129838A (en)	2007-05-31
SK5792003A3 (en)	2004-01-08
NO20032143L (no)	2003-07-07
CA2428642C (en)	2010-03-30
DE60144395D1 (de)	2011-05-19
PL206783B1 (pl)	2010-09-30
CZ20031657A3 (cs)	2003-10-15
KR20030059252A (ko)	2003-07-07
NZ526280A (en)	2006-02-24
BR0115344A (pt)	2003-08-26
AR031334A1 (es)	2003-09-17
IL155568A (en)	2010-02-17
GB0027779D0 (en)	2000-12-27
HUP0301619A2 (hu)	2003-09-29
EE200300232A (et)	2003-10-15
PL361881A1 (en)	2004-10-04
ZA200303547B (en)	2004-05-10
EA200300502A1 (ru)	2003-12-25
CA2428642A1 (en)	2002-05-23
EP1407030B1 (en)	2011-04-06
KR100856346B1 (ko)	2008-09-04
HRP20030377A2 (en)	2005-04-30
ECSP034573A (es)	2003-05-26
EA005163B1 (ru)	2004-12-30
BG107780A (bg)	2004-02-27
YU36103A (sh)	2006-05-25
WO2002040650A3 (en)	2003-12-31
ATE504652T1 (de)	2011-04-15
EP1407030A2 (en)	2004-04-14
UY27020A1 (es)	2002-07-31
HK1070097A1 (zh)	2005-06-10
CN1541271A (zh)	2004-10-27
JP2004520018A (ja)	2004-07-08

Publication	Publication Date	Title
Manosroi et al.	2001	Secretion of active recombinant human tissue plasminogen activator derivatives in Escherichia coli
US7087412B2 (en)	2006-08-08	Methods for large scale protein production in prokaryotes
US10597664B2 (en)	2020-03-24	Expression and purification of CRM proteins and related proteins, and protein domains
KR20030051821A (ko)	2003-06-25	원핵세포에서의 단백질 대량 생산 방법
UA75102C2 (en)	2006-03-15	METHODS FOR THE MASS PRODUCTION OF A RECOMBINANT DNA-DERIVED MOLECULES OF tPA OR K2S
US6955910B2 (en)	2005-10-18	Method for large scale production of recombinant DNA-derived TPA or K2S molecules
DK175020B1 (da)	2004-04-26	Fremgangsåde til udtrykkelse og ekstracellulær udskillelse af proteiner i G(-)bakterie, rekombinant DNA-konstruktion og plasmidvektor kodende herfor, samt G(-)bakterie indeholdende disse
Taheri et al.	2016	Engineering, expression and purification of a chimeric fibrin-specific streptokinase
Secchi et al.	2009	The superior folding of a RANTES analogue expressed in lactobacilli as compared to mammalian cells reveals a promising system to screen new RANTES mutants
AU2002221815A1 (en)	2002-08-01	Methods for large scale production of recombinant DNA-derived tPA or K2S molecules
Nguyen et al.	2012	Cloning, high-level expression, purification and characterization of a staphylokinase variant, SakøC, from Staphylococcus aureus QT08 in Escherichia coli BL21
US7829687B2 (en)	2010-11-09	Artificial disulfide isomerases and uses thereof
Vadhiya et al.	2025	Molecular identification and optimization of media components for enhanced production of staphylokinase produced by Staphylococcus aureus SAK42 from bovine milk
RU2495933C2 (ru)	2013-10-20	ПЛАЗМИДА ДЛЯ ЭКСПРЕССИИ В КЛЕТКАХ БАКТЕРИИ РОДА Escherichia ПРЕДШЕСТВЕННИКА РЕКОМБИНАНТНОГО ФРАГМЕНТА ТКАНЕВОГО АКТИВАТОРА ПЛАЗМИНОГЕНА (ТАП) ЧЕЛОВЕКА (РЕТЕПЛАЗЫ), БАКТЕРИЯ, ПРИНАДЛЕЖАЩАЯ К РОДУ Escherichia, - ПРОДУЦЕНТ ПРЕДШЕСТВЕННИКА РЕКОМБИНАНТНОГО ФРАГМЕНТА ТАП ЧЕЛОВЕКА (РЕТЕПЛАЗЫ) ИЛИ [-1]МЕТИОНИЛ-ФРАГМЕНТ ТАП ЧЕЛОВЕКА (РЕТЕПЛАЗЫ), ПРЕДШЕСТВЕННИК РЕКОМБИНАНТНОГО ФРАГМЕНТА ТАП ЧЕЛОВЕКА (РЕТЕПЛАЗЫ), СПОСОБ ПОЛУЧЕНИЯ ПРЕДШЕСТВЕННИКА РЕКОМБИНАНТНОГО ФРАГМЕНТА ТАП ЧЕЛОВЕКА (РЕТЕПЛАЗЫ)
RU2373281C2 (ru)	2009-11-20	Способ продукции рекомбинантной стафилокиназы при регулировании уровня кислорода
Bang et al.	2013	Production and on-column re-folding of human vascular endothelial growth factor 165 in Escherichia coli
Malik	2007	A novel strategy for the periplasmic production of heterologous proteins in E. coli
Swartz et al.	2000	Methods for producing heterologous disulfide bond-containing polypeptides in bacterial cells
HK1077848B (en)	2009-06-26	Methods for large scale protein production in prokaryotes
HK1070097B (en)	2010-02-19	Methods for large scale production of recombinant dna-derived tpa or k2s molecules