Characterization of a hemorrhagic factor, LHF-I, isolated from the bushmaster snake (Lachesis muta muta) venom.
Toxicon
; 33(12): 1653-67, 1995 Dec.
Article
en En
| MEDLINE
| ID: mdl-8866622
ABSTRACT
Hemorrhagic factor I (LHF-I) was previously purified from the venom of the bushmaster snake (Lachesis muta muta). In terms of biochemical and immunological properties, LHF-I is a glycoprotein (mol. wt 100,000, pI 4.7) consisting of two subunits; it loses its activity following mercaptoethanol treatment. LHF-I contains 0.7 g-atom zinc and 1.2 g-atom calcium per mole protein. The hemorrhagic and the proteinase activities are inhibited by EDTA; subsequent addition of Ca2+ or Mg2+ does not reverse the EDTA-induced inhibition of the hemorrhagic activity. The metalloenzyme does not hyrolyze arginine esters and is devoid of phospholipase A2 activity. It hydrolyzes the A alpha- > B beta-chain of fibrinogen without clot formation and hydrolyzes selectively the alpha-chain of fibrin, leaving the B beta- and tau-chains unaffected. Antibodies to the hemorrhagic factor in bushmaster venom were produced by immunizing rabbits with the purified protein. The antibody was purified by protein-A affinity chromatography. This antibody was also used to screen other Crotalinae venom samples for immunologically similar epitopes by ELISA assay. The purified antibody reacted only with LHF-I and two samples of bushmaster venom from different geographical locations.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Venenos de Crotálidos
Límite:
Animals
Idioma:
En
Revista:
Toxicon
Año:
1995
Tipo del documento:
Article
País de afiliación:
Brasil