I--isolation and electron microscope studies of a potent platelet-aggregating glycoprotein from the venom of Crotalus durissus cascavella.
Biochimie
; 65(7): 405-16, 1983 Jul.
Article
em En
| MEDLINE
| ID: mdl-6626587
ABSTRACT
A potent acid-soluble platelet-aggregating glycoprotein was purified from the venom of Crotalus durissus cascavella by molecular sieve chromatography on Sephadex G-75 and by adsorption onto Sepharose 4B gels at acidic pH. This new protein with an apparent Mr of 300,000 at acidic pH and containing a low amount of sugars is non-toxic for mice. Electron microscope studies showed that the platelet-aggregating glycoprotein appeared as regular rosettes of 150 A in diameter at acidic pH and underwent polymerization in rod-like particles in the presence of sodium chloride. This glycoprotein, probably hydrophobic, is dissociated into an active molecular form whose apparent Mr was 144,000; however, it is believed to still be a not totally dissociated molecule.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Glicoproteínas
/
Agregação Plaquetária
/
Venenos de Crotalídeos
/
Lectinas Tipo C
Limite:
Animals
Idioma:
En
Revista:
Biochimie
Ano de publicação:
1983
Tipo de documento:
Article