Purification and properties of the thrombin-like enzyme from the venom of Lachesis muta muta.
Int J Biochem
; 21(8): 863-71, 1989.
Article
en En
| MEDLINE
| ID: mdl-2583354
ABSTRACT
1. The coagulating enzyme of the Lachesis muta muta venom was purified to homogeneity by a combination of a gel filtration in Sephadex G-100 and affinity chromatography on agarose-agmatine resin. 2. Several forms of the enzyme were prepared by isoelectric focusing with pIs ranging from 3.1 to 5.0; the asialoenzyme focused as a narrow band at pH 8.7. SDS-PAGE analysis of the purified enzyme revealed a single broad band with apparent Mr of 41-47 kDa. 3. The enzyme cleaves only fibrinopeptide A from fibrinogen; it does not activate factor XIII and is devoid of kallikrein-like activity. 4. Kinetic properties of the enzyme were determined for representative synthetic chromogenic substrates and inhibitors.
Buscar en Google
Banco de datos:
MEDLINE
Asunto principal:
Trombina
/
Venenos de Crotálidos
Límite:
Animals
Idioma:
En
Año:
1989
Tipo del documento:
Article