NO314848B1 - Protein for inhibering av kollagenfremkalt blodplateaggregering, DNA som koder for proteinet, vektor som omfatter et slikt DNA, vertscelletransformert medvektoren, fremgangsmåter for fremstilling og rensing avproteinet, farmasöytiskpreparat - Google Patents
Protein for inhibering av kollagenfremkalt blodplateaggregering, DNA som koder for proteinet, vektor som omfatter et slikt DNA, vertscelletransformert medvektoren, fremgangsmåter for fremstilling og rensing avproteinet, farmasöytiskpreparat Download PDFInfo
- Publication number
- NO314848B1 NO314848B1 NO19940771A NO940771A NO314848B1 NO 314848 B1 NO314848 B1 NO 314848B1 NO 19940771 A NO19940771 A NO 19940771A NO 940771 A NO940771 A NO 940771A NO 314848 B1 NO314848 B1 NO 314848B1
- Authority
- NO
- Norway
- Prior art keywords
- protein
- seq
- dna
- inhibitor
- sequence
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 228
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 216
- 229920001436 collagen Polymers 0.000 title claims abstract description 85
- 108010035532 Collagen Proteins 0.000 title claims abstract description 81
- 102000008186 Collagen Human genes 0.000 title claims abstract description 81
- 208000010110 spontaneous platelet aggregation Diseases 0.000 title claims abstract description 30
- 238000000034 method Methods 0.000 title claims description 33
- 239000013598 vector Substances 0.000 title claims description 20
- 239000000825 pharmaceutical preparation Substances 0.000 title claims description 9
- 230000002401 inhibitory effect Effects 0.000 title abstract description 12
- 210000004881 tumor cell Anatomy 0.000 claims abstract description 28
- 206010061289 metastatic neoplasm Diseases 0.000 claims abstract description 18
- 206010028980 Neoplasm Diseases 0.000 claims abstract description 15
- 239000003814 drug Substances 0.000 claims abstract description 12
- 201000011510 cancer Diseases 0.000 claims abstract description 10
- 239000002299 complementary DNA Substances 0.000 claims description 50
- 150000001413 amino acids Chemical class 0.000 claims description 49
- 108020004414 DNA Proteins 0.000 claims description 47
- 238000004220 aggregation Methods 0.000 claims description 36
- 230000002776 aggregation Effects 0.000 claims description 36
- 230000000694 effects Effects 0.000 claims description 32
- 210000004027 cell Anatomy 0.000 claims description 31
- 230000005764 inhibitory process Effects 0.000 claims description 28
- 108091026890 Coding region Proteins 0.000 claims description 17
- 230000004048 modification Effects 0.000 claims description 11
- 238000012986 modification Methods 0.000 claims description 11
- 239000002773 nucleotide Substances 0.000 claims description 11
- 125000003729 nucleotide group Chemical group 0.000 claims description 11
- 229940079593 drug Drugs 0.000 claims description 10
- 238000004519 manufacturing process Methods 0.000 claims description 9
- 241000699800 Cricetinae Species 0.000 claims description 8
- 230000013595 glycosylation Effects 0.000 claims description 8
- 108010076504 Protein Sorting Signals Proteins 0.000 claims description 7
- 238000001962 electrophoresis Methods 0.000 claims description 7
- 238000002523 gelfiltration Methods 0.000 claims description 7
- 238000006206 glycosylation reaction Methods 0.000 claims description 7
- 238000004587 chromatography analysis Methods 0.000 claims description 6
- 239000003623 enhancer Substances 0.000 claims description 6
- 210000003292 kidney cell Anatomy 0.000 claims description 6
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 claims description 5
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 claims description 5
- 239000003085 diluting agent Substances 0.000 claims description 5
- 238000002360 preparation method Methods 0.000 claims description 5
- 230000004481 post-translational protein modification Effects 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 3
- 230000001154 acute effect Effects 0.000 claims 1
- 230000001225 therapeutic effect Effects 0.000 claims 1
- 241001414832 Meccus pallidipennis Species 0.000 abstract description 18
- 235000018102 proteins Nutrition 0.000 description 191
- 239000003112 inhibitor Substances 0.000 description 77
- 238000010804 cDNA synthesis Methods 0.000 description 47
- 108020004635 Complementary DNA Proteins 0.000 description 44
- 210000001772 blood platelet Anatomy 0.000 description 43
- 210000003296 saliva Anatomy 0.000 description 24
- 235000001014 amino acid Nutrition 0.000 description 23
- 239000013612 plasmid Substances 0.000 description 21
- 238000006243 chemical reaction Methods 0.000 description 19
- 229940046166 oligodeoxynucleotide Drugs 0.000 description 19
- 229920002684 Sepharose Polymers 0.000 description 15
- 239000000872 buffer Substances 0.000 description 15
- 238000012360 testing method Methods 0.000 description 15
- 108091028043 Nucleic acid sequence Proteins 0.000 description 14
- 239000012634 fragment Substances 0.000 description 14
- 150000001875 compounds Chemical class 0.000 description 13
- 230000029087 digestion Effects 0.000 description 13
- 208000010125 myocardial infarction Diseases 0.000 description 12
- 210000004623 platelet-rich plasma Anatomy 0.000 description 12
- 238000000746 purification Methods 0.000 description 12
- 108091008146 restriction endonucleases Proteins 0.000 description 12
- 208000007536 Thrombosis Diseases 0.000 description 11
- 101000783577 Dendroaspis angusticeps Thrombostatin Proteins 0.000 description 10
- 101000783578 Dendroaspis jamesoni kaimosae Dendroaspin Proteins 0.000 description 10
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
- 229940127218 antiplatelet drug Drugs 0.000 description 10
- 239000013604 expression vector Substances 0.000 description 10
- 239000000106 platelet aggregation inhibitor Substances 0.000 description 10
- 210000003079 salivary gland Anatomy 0.000 description 10
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 9
- 238000010367 cloning Methods 0.000 description 9
- 206010038563 Reocclusion Diseases 0.000 description 8
- 230000015572 biosynthetic process Effects 0.000 description 8
- 238000011534 incubation Methods 0.000 description 8
- 230000003993 interaction Effects 0.000 description 8
- 238000002955 isolation Methods 0.000 description 8
- 239000000523 sample Substances 0.000 description 8
- 206010027476 Metastases Diseases 0.000 description 7
- 230000003143 atherosclerotic effect Effects 0.000 description 7
- 210000004369 blood Anatomy 0.000 description 7
- 239000008280 blood Substances 0.000 description 7
- 238000001712 DNA sequencing Methods 0.000 description 6
- 108010049003 Fibrinogen Proteins 0.000 description 6
- 102000008946 Fibrinogen Human genes 0.000 description 6
- 241000238631 Hexapoda Species 0.000 description 6
- 241001414833 Triatoma Species 0.000 description 6
- 239000007983 Tris buffer Substances 0.000 description 6
- 238000010276 construction Methods 0.000 description 6
- 229940012952 fibrinogen Drugs 0.000 description 6
- 239000000499 gel Substances 0.000 description 6
- 239000011159 matrix material Substances 0.000 description 6
- 230000009401 metastasis Effects 0.000 description 6
- 230000002265 prevention Effects 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 238000007363 ring formation reaction Methods 0.000 description 6
- 238000006467 substitution reaction Methods 0.000 description 6
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 6
- 108700026244 Open Reading Frames Proteins 0.000 description 5
- 238000012408 PCR amplification Methods 0.000 description 5
- 239000011543 agarose gel Substances 0.000 description 5
- 238000002399 angioplasty Methods 0.000 description 5
- 239000003937 drug carrier Substances 0.000 description 5
- 230000006870 function Effects 0.000 description 5
- 238000009396 hybridization Methods 0.000 description 5
- 239000003550 marker Substances 0.000 description 5
- 238000012216 screening Methods 0.000 description 5
- 230000028327 secretion Effects 0.000 description 5
- 238000012163 sequencing technique Methods 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 241000894007 species Species 0.000 description 5
- 238000003786 synthesis reaction Methods 0.000 description 5
- BSYNRYMUTXBXSQ-UHFFFAOYSA-N Aspirin Chemical compound CC(=O)OC1=CC=CC=C1C(O)=O BSYNRYMUTXBXSQ-UHFFFAOYSA-N 0.000 description 4
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 4
- PHEDXBVPIONUQT-UHFFFAOYSA-N Cocarcinogen A1 Natural products CCCCCCCCCCCCCC(=O)OC1C(C)C2(O)C3C=C(C)C(=O)C3(O)CC(CO)=CC2C2C1(OC(C)=O)C2(C)C PHEDXBVPIONUQT-UHFFFAOYSA-N 0.000 description 4
- 102000029816 Collagenase Human genes 0.000 description 4
- 108060005980 Collagenase Proteins 0.000 description 4
- 108010038807 Oligopeptides Proteins 0.000 description 4
- 102000015636 Oligopeptides Human genes 0.000 description 4
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 4
- 108010001014 Plasminogen Activators Proteins 0.000 description 4
- 102000001938 Plasminogen Activators Human genes 0.000 description 4
- 229960001138 acetylsalicylic acid Drugs 0.000 description 4
- 239000003146 anticoagulant agent Substances 0.000 description 4
- 229960004676 antithrombotic agent Drugs 0.000 description 4
- 239000003153 chemical reaction reagent Substances 0.000 description 4
- 229960002424 collagenase Drugs 0.000 description 4
- 231100000673 dose–response relationship Toxicity 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
- 238000000605 extraction Methods 0.000 description 4
- 238000001727 in vivo Methods 0.000 description 4
- 238000003780 insertion Methods 0.000 description 4
- 230000037431 insertion Effects 0.000 description 4
- 230000003902 lesion Effects 0.000 description 4
- 210000004962 mammalian cell Anatomy 0.000 description 4
- 108020004999 messenger RNA Proteins 0.000 description 4
- 229920001542 oligosaccharide Polymers 0.000 description 4
- 150000002482 oligosaccharides Chemical class 0.000 description 4
- PHEDXBVPIONUQT-RGYGYFBISA-N phorbol 13-acetate 12-myristate Chemical compound C([C@]1(O)C(=O)C(C)=C[C@H]1[C@@]1(O)[C@H](C)[C@H]2OC(=O)CCCCCCCCCCCCC)C(CO)=C[C@H]1[C@H]1[C@]2(OC(C)=O)C1(C)C PHEDXBVPIONUQT-RGYGYFBISA-N 0.000 description 4
- 229940127126 plasminogen activator Drugs 0.000 description 4
- 230000037452 priming Effects 0.000 description 4
- 108090000765 processed proteins & peptides Proteins 0.000 description 4
- 238000001742 protein purification Methods 0.000 description 4
- RXWNCPJZOCPEPQ-NVWDDTSBSA-N puromycin Chemical compound C1=CC(OC)=CC=C1C[C@H](N)C(=O)N[C@H]1[C@@H](O)[C@H](N2C3=NC=NC(=C3N=C2)N(C)C)O[C@@H]1CO RXWNCPJZOCPEPQ-NVWDDTSBSA-N 0.000 description 4
- 239000000725 suspension Substances 0.000 description 4
- 230000014616 translation Effects 0.000 description 4
- KKJUPNGICOCCDW-UHFFFAOYSA-N 7-N,N-Dimethylamino-1,2,3,4,5-pentathiocyclooctane Chemical compound CN(C)C1CSSSSSC1 KKJUPNGICOCCDW-UHFFFAOYSA-N 0.000 description 3
- 108010048623 Collagen Receptors Proteins 0.000 description 3
- 102000009268 Collagen Receptors Human genes 0.000 description 3
- 239000003298 DNA probe Substances 0.000 description 3
- 241000288900 Desmodus rotundus Species 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- 108010017642 Integrin alpha2beta1 Proteins 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 3
- 206010040047 Sepsis Diseases 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 108090000190 Thrombin Proteins 0.000 description 3
- 108090000631 Trypsin Proteins 0.000 description 3
- 102000004142 Trypsin Human genes 0.000 description 3
- 101710099833 Venom protein Proteins 0.000 description 3
- 230000001464 adherent effect Effects 0.000 description 3
- 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 3
- 229960000723 ampicillin Drugs 0.000 description 3
- 230000004071 biological effect Effects 0.000 description 3
- 210000004204 blood vessel Anatomy 0.000 description 3
- 239000003636 conditioned culture medium Substances 0.000 description 3
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 3
- HQPMKSGTIOYHJT-UHFFFAOYSA-N ethane-1,2-diol;propane-1,2-diol Chemical compound OCCO.CC(O)CO HQPMKSGTIOYHJT-UHFFFAOYSA-N 0.000 description 3
- 230000007246 mechanism Effects 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 238000010369 molecular cloning Methods 0.000 description 3
- 238000002703 mutagenesis Methods 0.000 description 3
- 231100000350 mutagenesis Toxicity 0.000 description 3
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 3
- 229920001993 poloxamer 188 Polymers 0.000 description 3
- 229920002401 polyacrylamide Polymers 0.000 description 3
- 229920001184 polypeptide Polymers 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 230000002797 proteolythic effect Effects 0.000 description 3
- 230000002829 reductive effect Effects 0.000 description 3
- 230000010076 replication Effects 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 239000003998 snake venom Substances 0.000 description 3
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 229960004072 thrombin Drugs 0.000 description 3
- 230000001732 thrombotic effect Effects 0.000 description 3
- 230000009466 transformation Effects 0.000 description 3
- 238000013519 translation Methods 0.000 description 3
- 239000012588 trypsin Substances 0.000 description 3
- ZABMJSAHPWHMNM-QCOJBMJGSA-N (2s)-6-amino-2-[[(2s)-1-[2-[[(2s)-1-[(2s)-4-carboxy-2-[[2-[[(2s)-1-[(2s)-2,6-diaminohexanoyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]butanoyl]pyrrolidine-2-carbonyl]amino]acetyl]pyrrolidine-2-carbonyl]amino]hexanoic acid Chemical compound NCCCC[C@H](N)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N1[C@H](C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CCCCN)C(O)=O)CCC1 ZABMJSAHPWHMNM-QCOJBMJGSA-N 0.000 description 2
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 2
- 206010002388 Angina unstable Diseases 0.000 description 2
- 208000037260 Atherosclerotic Plaque Diseases 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- 108091033380 Coding strand Proteins 0.000 description 2
- 102000053602 DNA Human genes 0.000 description 2
- 108020003215 DNA Probes Proteins 0.000 description 2
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 2
- 102100031780 Endonuclease Human genes 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 2
- 241000545744 Hirudinea Species 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 101001024703 Homo sapiens Nck-associated protein 5 Proteins 0.000 description 2
- GRRNUXAQVGOGFE-UHFFFAOYSA-N Hygromycin-B Natural products OC1C(NC)CC(N)C(O)C1OC1C2OC3(C(C(O)C(O)C(C(N)CO)O3)O)OC2C(O)C(CO)O1 GRRNUXAQVGOGFE-UHFFFAOYSA-N 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 241000713883 Myeloproliferative sarcoma virus Species 0.000 description 2
- LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 description 2
- 102100036946 Nck-associated protein 5 Human genes 0.000 description 2
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 2
- 102000006382 Ribonucleases Human genes 0.000 description 2
- 108010083644 Ribonucleases Proteins 0.000 description 2
- 108091081024 Start codon Proteins 0.000 description 2
- 108010023197 Streptokinase Proteins 0.000 description 2
- 101710129367 Sugar transporter SWEET1 Proteins 0.000 description 2
- 108020005038 Terminator Codon Proteins 0.000 description 2
- 208000007814 Unstable Angina Diseases 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 230000000879 anti-atherosclerotic effect Effects 0.000 description 2
- 239000013602 bacteriophage vector Substances 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 239000002775 capsule Substances 0.000 description 2
- 150000001768 cations Chemical class 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 239000003638 chemical reducing agent Substances 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- XVOYSCVBGLVSOL-UHFFFAOYSA-N cysteic acid Chemical compound OC(=O)C(N)CS(O)(=O)=O XVOYSCVBGLVSOL-UHFFFAOYSA-N 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 239000005546 dideoxynucleotide Substances 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 210000003038 endothelium Anatomy 0.000 description 2
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 2
- 229960005542 ethidium bromide Drugs 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- 230000020764 fibrinolysis Effects 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 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 2
- 210000002288 golgi apparatus Anatomy 0.000 description 2
- 230000023597 hemostasis Effects 0.000 description 2
- GRRNUXAQVGOGFE-NZSRVPFOSA-N hygromycin B Chemical compound O[C@@H]1[C@@H](NC)C[C@@H](N)[C@H](O)[C@H]1O[C@H]1[C@H]2O[C@@]3([C@@H]([C@@H](O)[C@@H](O)[C@@H](C(N)CO)O3)O)O[C@H]2[C@@H](O)[C@@H](CO)O1 GRRNUXAQVGOGFE-NZSRVPFOSA-N 0.000 description 2
- 229940097277 hygromycin b Drugs 0.000 description 2
- 108010002685 hygromycin-B kinase Proteins 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 108091006086 inhibitor proteins Proteins 0.000 description 2
- 201000004332 intermediate coronary syndrome Diseases 0.000 description 2
- 210000003734 kidney Anatomy 0.000 description 2
- 108010055353 lysyl-prolyl-glycyl-glutamyl-prolyl-glycyl-prolyl-lysine Proteins 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 201000001441 melanoma Diseases 0.000 description 2
- 210000004379 membrane Anatomy 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 239000008024 pharmaceutical diluent Substances 0.000 description 2
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
- 230000008488 polyadenylation Effects 0.000 description 2
- 229920001296 polysiloxane Polymers 0.000 description 2
- 229950010131 puromycin Drugs 0.000 description 2
- 239000002464 receptor antagonist Substances 0.000 description 2
- 229940044551 receptor antagonist Drugs 0.000 description 2
- 238000002741 site-directed mutagenesis Methods 0.000 description 2
- 229960005202 streptokinase Drugs 0.000 description 2
- 239000002396 thromboxane receptor blocking agent Substances 0.000 description 2
- 238000001890 transfection Methods 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- 101710175516 14 kDa zinc-binding protein Proteins 0.000 description 1
- VGONTNSXDCQUGY-RRKCRQDMSA-N 2'-deoxyinosine Chemical compound C1[C@H](O)[C@@H](CO)O[C@H]1N1C(N=CNC2=O)=C2N=C1 VGONTNSXDCQUGY-RRKCRQDMSA-N 0.000 description 1
- BHNQPLPANNDEGL-UHFFFAOYSA-N 2-(4-octylphenoxy)ethanol Chemical compound CCCCCCCCC1=CC=C(OCCO)C=C1 BHNQPLPANNDEGL-UHFFFAOYSA-N 0.000 description 1
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 1
- 108010039627 Aprotinin Proteins 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-M Bicarbonate Chemical compound OC([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-M 0.000 description 1
- 239000005996 Blood meal Substances 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 206010006187 Breast cancer Diseases 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 108010038061 Chymotrypsinogen Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 229940123228 Collagen inhibitor Drugs 0.000 description 1
- 241000701022 Cytomegalovirus Species 0.000 description 1
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 description 1
- 230000004544 DNA amplification Effects 0.000 description 1
- 238000007900 DNA-DNA hybridization Methods 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 description 1
- 108010054576 Deoxyribonuclease EcoRI Proteins 0.000 description 1
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 241000193159 Hathewaya histolytica Species 0.000 description 1
- 241000237902 Hirudo medicinalis Species 0.000 description 1
- 241000701024 Human betaherpesvirus 5 Species 0.000 description 1
- 102100024319 Intestinal-type alkaline phosphatase Human genes 0.000 description 1
- 101710184243 Intestinal-type alkaline phosphatase Proteins 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- GDBQQVLCIARPGH-UHFFFAOYSA-N Leupeptin Natural products CC(C)CC(NC(C)=O)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N GDBQQVLCIARPGH-UHFFFAOYSA-N 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 description 1
- 239000006142 Luria-Bertani Agar Substances 0.000 description 1
- 239000006137 Luria-Bertani broth Substances 0.000 description 1
- 241000713869 Moloney murine leukemia virus Species 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 241000233622 Phytophthora infestans Species 0.000 description 1
- 206010050661 Platelet aggregation inhibition Diseases 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 102000003923 Protein Kinase C Human genes 0.000 description 1
- 108090000315 Protein Kinase C Proteins 0.000 description 1
- 229940123924 Protein kinase C inhibitor Drugs 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 241000722249 Rhodnius prolixus Species 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 108700009124 Transcription Initiation Site Proteins 0.000 description 1
- 241001249485 Triatoma dimidiata Species 0.000 description 1
- 241000351625 Triatoma maculata Species 0.000 description 1
- 241001210412 Triatominae Species 0.000 description 1
- 241000223109 Trypanosoma cruzi Species 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 108091023045 Untranslated Region Proteins 0.000 description 1
- HMNZFMSWFCAGGW-XPWSMXQVSA-N [3-[hydroxy(2-hydroxyethoxy)phosphoryl]oxy-2-[(e)-octadec-9-enoyl]oxypropyl] (e)-octadec-9-enoate Chemical compound CCCCCCCC\C=C\CCCCCCCC(=O)OCC(COP(O)(=O)OCCO)OC(=O)CCCCCCC\C=C\CCCCCCCC HMNZFMSWFCAGGW-XPWSMXQVSA-N 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 238000012197 amplification kit Methods 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 230000002001 anti-metastasis Effects 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 229960004405 aprotinin Drugs 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 108010058966 bacteriophage T7 induced DNA polymerase Proteins 0.000 description 1
- 210000002469 basement membrane Anatomy 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 230000001851 biosynthetic effect Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 108010051489 calin Proteins 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
- 238000007887 coronary angioplasty Methods 0.000 description 1
- 239000012228 culture supernatant 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
- 230000009089 cytolysis Effects 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 210000000172 cytosol Anatomy 0.000 description 1
- RGWHQCVHVJXOKC-SHYZEUOFSA-J dCTP(4-) Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-J 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- VGONTNSXDCQUGY-UHFFFAOYSA-N desoxyinosine Natural products C1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 VGONTNSXDCQUGY-UHFFFAOYSA-N 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 230000000001 effect on platelet aggregation Effects 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 239000002319 fibrinogen receptor antagonist Substances 0.000 description 1
- 239000003527 fibrinolytic agent Substances 0.000 description 1
- 230000003480 fibrinolytic effect Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000005189 flocculation Methods 0.000 description 1
- 230000016615 flocculation Effects 0.000 description 1
- 230000037406 food intake Effects 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 238000002825 functional assay Methods 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 108091005608 glycosylated proteins Proteins 0.000 description 1
- 102000035122 glycosylated proteins Human genes 0.000 description 1
- ZJYYHGLJYGJLLN-UHFFFAOYSA-N guanidinium thiocyanate Chemical compound SC#N.NC(N)=N ZJYYHGLJYGJLLN-UHFFFAOYSA-N 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 229960002240 iloprost Drugs 0.000 description 1
- HIFJCPQKFCZDDL-ACWOEMLNSA-N iloprost Chemical compound C1\C(=C/CCCC(O)=O)C[C@@H]2[C@@H](/C=C/[C@@H](O)C(C)CC#CC)[C@H](O)C[C@@H]21 HIFJCPQKFCZDDL-ACWOEMLNSA-N 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- GDBQQVLCIARPGH-ULQDDVLXSA-N leupeptin Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C=O)CCCN=C(N)N GDBQQVLCIARPGH-ULQDDVLXSA-N 0.000 description 1
- 108010052968 leupeptin Proteins 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 238000004020 luminiscence type Methods 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 210000003712 lysosome Anatomy 0.000 description 1
- 230000001868 lysosomic effect Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 230000001394 metastastic effect Effects 0.000 description 1
- 229940098779 methanesulfonic acid Drugs 0.000 description 1
- AFVFQIVMOAPDHO-UHFFFAOYSA-N methanesulfonic acid Substances CS(O)(=O)=O AFVFQIVMOAPDHO-UHFFFAOYSA-N 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 229940019331 other antithrombotic agent in atc Drugs 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 239000008177 pharmaceutical agent Substances 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 150000004633 phorbol derivatives Chemical class 0.000 description 1
- 239000002644 phorbol ester Substances 0.000 description 1
- 210000002381 plasma Anatomy 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 108010081580 platelet adhesion inhibitor Proteins 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000011533 pre-incubation Methods 0.000 description 1
- 230000002947 procoagulating effect Effects 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 230000000644 propagated effect Effects 0.000 description 1
- 239000003881 protein kinase C inhibitor Substances 0.000 description 1
- 230000009145 protein modification Effects 0.000 description 1
- 108010045647 puromycin N-acetyltransferase Proteins 0.000 description 1
- 239000011535 reaction buffer Substances 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 210000003660 reticulum Anatomy 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000010187 selection method Methods 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 230000019491 signal transduction Effects 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
- 238000001179 sorption measurement Methods 0.000 description 1
- 230000002269 spontaneous effect Effects 0.000 description 1
- 230000007480 spreading Effects 0.000 description 1
- 238000003892 spreading Methods 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- RZWIIPASKMUIAC-VQTJNVASSA-N thromboxane Chemical compound CCCCCCCC[C@H]1OCCC[C@@H]1CCCCCCC RZWIIPASKMUIAC-VQTJNVASSA-N 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- 238000005199 ultracentrifugation Methods 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
- C07K14/43563—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from insects
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- 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
-
- 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)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Zoology (AREA)
- General Chemical & Material Sciences (AREA)
- Veterinary Medicine (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Diabetes (AREA)
- Hematology (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Insects & Arthropods (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US75621191A | 1991-09-05 | 1991-09-05 | |
US81488491A | 1991-12-31 | 1991-12-31 | |
US91438392A | 1992-07-17 | 1992-07-17 | |
PCT/EP1992/002052 WO1993005150A1 (en) | 1991-09-05 | 1992-09-04 | Collagen-induced platelet aggregation inhibitor |
Publications (3)
Publication Number | Publication Date |
---|---|
NO940771D0 NO940771D0 (no) | 1994-03-04 |
NO940771L NO940771L (no) | 1994-03-04 |
NO314848B1 true NO314848B1 (no) | 2003-06-02 |
Family
ID=27419489
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO19940771A NO314848B1 (no) | 1991-09-05 | 1994-03-04 | Protein for inhibering av kollagenfremkalt blodplateaggregering, DNA som koder for proteinet, vektor som omfatter et slikt DNA, vertscelletransformert medvektoren, fremgangsmåter for fremstilling og rensing avproteinet, farmasöytiskpreparat |
Country Status (16)
Country | Link |
---|---|
EP (1) | EP0530937B1 (de) |
JP (2) | JPH07506959A (de) |
KR (1) | KR100232683B1 (de) |
AT (1) | ATE169674T1 (de) |
AU (1) | AU672584B2 (de) |
CA (1) | CA2117174A1 (de) |
DE (1) | DE69226580T2 (de) |
DK (1) | DK0530937T3 (de) |
ES (1) | ES2121817T3 (de) |
FI (1) | FI112801B (de) |
HU (1) | HU218830B (de) |
IL (4) | IL103065A (de) |
NO (1) | NO314848B1 (de) |
NZ (1) | NZ244246A (de) |
RU (1) | RU2128705C1 (de) |
WO (1) | WO1993005150A1 (de) |
Families Citing this family (12)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
RU2186110C2 (ru) * | 1994-09-12 | 2002-07-27 | Шеринг Аг | Рекомбинантный белок asp-паллидипин, способ его производства и очистки, вектор, штамм, фармацевтическая композиция |
GB2304048A (en) * | 1995-08-12 | 1997-03-12 | John William Carson | Medicament containing saliva extract |
JP3837519B2 (ja) | 2002-10-02 | 2006-10-25 | 国立大学法人三重大学 | 血小板凝集阻害活性を有するブラジルサシガメ由来のTi−3蛋白質 |
JP3837518B2 (ja) | 2002-10-02 | 2006-10-25 | 国立大学法人三重大学 | 血小板凝集阻害活性を有するブラジルサシガメ由来のTi−4蛋白質 |
AU2003227721A1 (en) * | 2003-05-02 | 2004-11-23 | Paion Gmbh | Intravenous injection of non-neurotoxic plasminogen activators for the treatment of stroke |
ATE384735T1 (de) * | 2003-05-21 | 2008-02-15 | Ares Trading Sa | Verfahren zur chromatographischen analyse einer proteinlösung |
EP1760092A1 (de) * | 2005-08-26 | 2007-03-07 | Applied Research Systems ARS Holding N.V. | System für Screening von Zellen mit hoher Expression von einem interessierenden Protein |
WO2007038749A2 (en) | 2005-09-28 | 2007-04-05 | Biovascular, Inc. | Methods and compositions for blocking platelet and cell adhesion, cell migration and inflammation |
JP5332178B2 (ja) * | 2007-11-02 | 2013-11-06 | 東洋紡株式会社 | 多色ルシフェラーゼの検出方法 |
JP5747370B2 (ja) * | 2009-03-31 | 2015-07-15 | 国立大学法人浜松医科大学 | 高病原性口腔細菌の高感度検出法 |
CN109125355B (zh) * | 2018-08-03 | 2022-07-08 | 昆明医科大学第一附属医院 | 心脉隆抗血小板及抗血栓药理应用 |
CN110327994B (zh) * | 2019-07-11 | 2020-12-08 | 北京理工大学 | 一种多维微流控电泳芯片及检测装置,检测方法 |
-
1992
- 1992-09-04 CA CA002117174A patent/CA2117174A1/en not_active Abandoned
- 1992-09-04 RU RU94045930A patent/RU2128705C1/ru not_active IP Right Cessation
- 1992-09-04 JP JP5500350A patent/JPH07506959A/ja not_active Withdrawn
- 1992-09-04 HU HU9400662A patent/HU218830B/hu not_active IP Right Cessation
- 1992-09-04 WO PCT/EP1992/002052 patent/WO1993005150A1/en active IP Right Grant
- 1992-09-04 KR KR1019940700723A patent/KR100232683B1/ko not_active IP Right Cessation
- 1992-09-04 IL IL10306592A patent/IL103065A/en not_active IP Right Cessation
- 1992-09-04 DK DK92250245T patent/DK0530937T3/da active
- 1992-09-04 AU AU25022/92A patent/AU672584B2/en not_active Ceased
- 1992-09-04 IL IL11949192A patent/IL119491A/xx not_active IP Right Cessation
- 1992-09-04 AT AT92250245T patent/ATE169674T1/de not_active IP Right Cessation
- 1992-09-04 ES ES92250245T patent/ES2121817T3/es not_active Expired - Lifetime
- 1992-09-04 DE DE69226580T patent/DE69226580T2/de not_active Expired - Fee Related
- 1992-09-04 EP EP92250245A patent/EP0530937B1/de not_active Expired - Lifetime
- 1992-09-07 NZ NZ244246A patent/NZ244246A/en unknown
-
1994
- 1994-03-04 FI FI941052A patent/FI112801B/fi not_active IP Right Cessation
- 1994-03-04 NO NO19940771A patent/NO314848B1/no unknown
-
1996
- 1996-10-25 IL IL11949296A patent/IL119492A0/xx not_active IP Right Cessation
- 1996-10-25 IL IL11949196A patent/IL119491A0/xx unknown
-
2003
- 2003-04-22 JP JP2003117673A patent/JP2003313199A/ja not_active Ceased
Also Published As
Publication number | Publication date |
---|---|
HU218830B (hu) | 2000-12-28 |
DE69226580T2 (de) | 1999-03-04 |
KR100232683B1 (ko) | 1999-12-01 |
NO940771D0 (no) | 1994-03-04 |
HUT70271A (en) | 1995-09-28 |
DK0530937T3 (da) | 1999-05-10 |
IL103065A0 (en) | 1993-02-21 |
AU672584B2 (en) | 1996-10-10 |
WO1993005150A1 (en) | 1993-03-18 |
EP0530937B1 (de) | 1998-08-12 |
RU2128705C1 (ru) | 1999-04-10 |
RU94045930A (ru) | 1996-07-20 |
IL119491A0 (en) | 1997-01-10 |
DE69226580D1 (de) | 1998-09-17 |
JP2003313199A (ja) | 2003-11-06 |
ATE169674T1 (de) | 1998-08-15 |
NZ244246A (en) | 1994-03-25 |
IL103065A (en) | 2001-11-25 |
IL119491A (en) | 2000-11-21 |
HU9400662D0 (en) | 1994-06-28 |
AU2502292A (en) | 1993-04-05 |
FI112801B (fi) | 2004-01-15 |
NO940771L (no) | 1994-03-04 |
FI941052A0 (fi) | 1994-03-04 |
CA2117174A1 (en) | 1993-03-18 |
EP0530937A1 (de) | 1993-03-10 |
FI941052A (fi) | 1994-03-04 |
IL119492A0 (en) | 1997-01-10 |
ES2121817T3 (es) | 1998-12-16 |
JPH07506959A (ja) | 1995-08-03 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
US5759542A (en) | Compositions and methods for the delivery of drugs by platelets for the treatment of cardiovascular and other diseases | |
JP3136551B2 (ja) | インターロイキン1β前駆体変換酵素をコードするDNA | |
JP3051995B2 (ja) | 酸化抵抗性トロンボモジュリン類縁体 | |
DK176140B1 (da) | Flagermusspyt-plasminogenaktivatorer | |
NO314848B1 (no) | Protein for inhibering av kollagenfremkalt blodplateaggregering, DNA som koder for proteinet, vektor som omfatter et slikt DNA, vertscelletransformert medvektoren, fremgangsmåter for fremstilling og rensing avproteinet, farmasöytiskpreparat | |
RU2186110C2 (ru) | Рекомбинантный белок asp-паллидипин, способ его производства и очистки, вектор, штамм, фармацевтическая композиция | |
AU708102B2 (en) | Chimeric MCP and DAF proteins with cell surface localizing domain | |
US5589360A (en) | Polypeptide, DNA fragment encoding the same, drug composition containing the same and process for producing the same | |
MXPA97001720A (en) | Process for the manufacture of a modified palidipine, inhibitor of platelet aggregation induced by colag | |
US5756454A (en) | Collagen-induced platelet aggregation inhibitor | |
JPH10215885A (ja) | 新規lep | |
CA2150909A1 (en) | Clotting inhibitor made from protostomia saliva | |
US5801017A (en) | Production of recombinant factor Xa inhibitor of leech Hirudo medicinalis | |
AU4581200A (en) | Protease activated receptor 2 variants | |
JP2002125671A (ja) | 新規rsbU−1 | |
US20040091887A1 (en) | Mucroslysin and its gene | |
JPH10337188A (ja) | 新規greA |