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Titolo:
Isolation and characterization of an arginine ester hydrolase from Bothrops jararacussu venom which induces contractions of the isolated rat uterus
Autore:
Andriao-Escarso, SH; Soares, AM; Rodrigues, VM; Mancin, AC; Reis, ML; Ballejo, G; Giglio, JR;
Indirizzi:
Univ Sao Paulo, Dept Bioquim, BR-14049900 Ribeirao Preto, SP, Brazil Univ Sao Paulo Ribeirao Preto SP Brazil BR-14049900 BCo Preto, SP, Brazil Univzilo Paulo, Dept Farmacol, Fac Med, BR-14049900 Ribeirao Preto, SP, Bra Univ Sao Paulo Ribeirao Preto SP Brazil BR-14049900 BCirao Preto, SP, Bra UnivPreto,aulo, Farmacol Lab, Fac Ciencias Farmaceut, BR-14049900 RibeiraoUniv Sao Paulo Ribeirao Preto SP Brazil BR-14049900 BCR-14049900 Ribeirao
Titolo Testata:
BIOCHEMISTRY AND MOLECULAR BIOLOGY INTERNATIONAL
fascicolo: 4, volume: 47, anno: 1999,
pagine: 699 - 706
SICI:
1039-9712(199904)47:4<699:IACOAA>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
KININ;
Keywords:
snake venom; arginine ester hydrolase; protease; uterus contraction;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Giglio, JR Univ Sao Paulo, Dept Bioquim, BR-14049900 Ribeirao Preto, SP, Brazil Univ Sao Paulo Ribeirao Preto SP Brazil BR-14049900 BC, Brazil
Citazione:
S.H. Andriao-Escarso et al., "Isolation and characterization of an arginine ester hydrolase from Bothrops jararacussu venom which induces contractions of the isolated rat uterus", BIOC MOL B, 47(4), 1999, pp. 699-706

Abstract

The isolation and partial characterization of a serine protease with arginine eater hydrolase activity from Bothrops jararacussu snake venom are described. The purification procedure consisted of a gel filtration of the crude venom on Sephadex G-75 followed by an ion-exchange chromatography of the active fraction on DEAE-cellulose and a rechromatography on Bio-Rex 70 resin. The esterase fraction (DI-III), M-r = 25,000 by SDS-PAGE, showed proteolytic activity on fibrinogen and casein. After 2hr incubation, the A alpha and B beta chains of fibrinogen were intensely hydrolysed, while the gamma chain kept apparentely intact, even after 20hr of incubation. In spite of that, DI-III did not clot fibrinogen. DI-III induced edema in the rat paw. Although unable to release bradykinin, it induced contractions of the isolated rat uterus. DI-III did not catalyse the hydrolysis of bradykinin. Its arginine ester hydrolase activity was completely inhibited by diisopropyl fluorophosphate after 1 hr incubation, but not by phenylmethylsulfonyl fluorideunder the same conditions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 10:20:37