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Titolo:
PURIFICATION AND CHARACTERIZATION OF PLATELET-AGGREGATION INHIBITORS FROM SNARE VENOMS
Autore:
TRIKHA M; ROTE WE; MANLEY PJ; LUCCHESI BR; MARKLAND FS;
Indirizzi:
UNIV SO CALIF,SCH MED,DEPT BIOCHEM & MOLEC BIOL,CRL 106 LOS ANGELES CA 90033 UNIV SO CALIF,SCH MED,DEPT BIOCHEM & MOLEC BIOL LOS ANGELES CA 90033 UNIV MICHIGAN,SCH MED,DEPT PHARMACOL ANN ARBOR MI 48109
Titolo Testata:
Thrombosis research
fascicolo: 1, volume: 73, anno: 1994,
pagine: 39 - 52
SICI:
0049-3848(1994)73:1<39:PACOPI>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
ARG-GLY-ASP; PLASMINOGEN-ACTIVATOR; SNAKE-VENOMS; PROTEINS; IIIA; FIBRINOGEN; VIPER; MODEL; IIB; METALLOPROTEINASE;
Keywords:
PLATELET AGGREGATION INHIBITORS; PROTEIN PURIFICATION; SNAKE VENOMS; GPIIB/IIIA; FIBRINOGEN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
M. Trikha et al., "PURIFICATION AND CHARACTERIZATION OF PLATELET-AGGREGATION INHIBITORS FROM SNARE VENOMS", Thrombosis research, 73(1), 1994, pp. 39-52

Abstract

Proteins that inhibit glycoprotein (GP) IIb/IIIa mediated platelet aggregation have been purified from the venom of two snake species. A small platelet aggregation inhibitor (pl.AI), multisquamatin (Mr=5,700),was purified from Echis multisquamatus venom by hydrophobic interaction HPLC and two steps on C18 reverse phase HPLC. A larger pl.AI, contortrostatin (Mr=15,000), was purified by a similar HPLC procedure from the venom of Agkistrodon contortrix contortrix. Both pl.AIs inhibit ADP-induced human, canine and rabbit platelet aggregation using plateletrich plasma (PRP). Multisquamatin has an IC50 of 97 nM, 281 nM and 333 nM for human, canine and rabbit PRP, respectively. Contortrostatin has an IC50 of 49 nM, 120 nM and 1,150 nM for human, canine rabbit PRP,respectively. In a competitive binding assay using I-125-7E3 (a monoclonal antibody to GPIIb/IIIa that inhibits platelet aggregation) both contortrostatin and multisquamatin demonstrated GPIIb/IIIa specific binding to human and canine platelets. The IC50 for contortrostatin displacement of 7E3 binding to human and canine GPIIb-IIIa is 27 nM and 16nM, respectively and for multisquamatin it is 3 nM and 63 nM, respectively. Our results indicate that both pl.AIs inhibit platelet aggregation by binding with high affinity to GPIIb/IIIa.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 04:28:10