Purificação e caracterização de uma proteina (SIII-3rp) do veneno de Bothrops alternatus que se liga ao fator de von Willebrand (vwF)

AUTOR(ES)
DATA DE PUBLICAÇÃO

1995

RESUMO

Botrocetin is a platelet coagglutin described in Bothrops jararaca venon suggested as a substitute for ristocetin as a mediator of the interaction between GPIb-IX complex and the von Willebrand factor (vWF) that lead to platelet agglutination (Read et al., 1978). A single chain and a two chain botrocetin were described in B. jararaca venon (Fujimura et al., 1991a). Two chain botrocetin is highly homologous in its aminoacid sequence to alboaggregin-B (isolated from the venom of Trimeresus albolabris) a protein which directly agglutinates platelets by binding to a site on platelet membrane GPIb- IX dose to or identical with the site for vWF binding (Peng et al., 1991) .lu this work we report the purification and isolation of a protein (SIII3rp) from Bothrops alternatus venon, through procedures of gel filtration, ion exchange chromatography and HPLC reverse phase chromatography with a C 18 column. The purified protein which inhibits the ristocetin binding to vWF, presented a sillgle band (28 kDa) in non denaturing conditions in 12,5% PAGESDS; after reduction with 0,1M DTT, a 15kDa band was observed. Automatic microsequencing of this proteill was performed on a Applied Biosystem 477 automatic model sequencer with liquid phase pulse. The N-termillal sequence obtained DCPSDWSPYEG presented 82% homology to the first elevell residues of the a and b chains of the heterodimeric botrocetin

ASSUNTO(S)

proteinas venenos hemostase

ACESSO AO ARTIGO

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