The complete amino acid sequence of the high molecular mass hemorrhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis.

摘要: Hemorrhage is a common occurrence in victim bitten by crotalid and viperid snakes, hemorrhagic components these various venoms have been isolated characterized. Previously, we shown that low molecular weight protein (HR2a, 202 amino acid residues) from the venom of Trimeresurus flavoviridis member new subfamily metalloproteinases. We now report complete sequence high mass same venom. This protein, HR1B, mosaic composed 416 residues containing four asparagine-linked oligosaccharide chains. The amino-terminal half (residues 1-203) HR1B contains metalloproteinase domain, which 62% identical to HR2a 52% toxin d Crotalus atrox most interesting finding middle region 204-300) shows striking similarity disintegrins, Arg-Gly-Asp-containing platelet aggregation inhibitors, recently found several viper venoms. Interestingly, however, this does not contain Arg-Gly-Asp known be putative binding site disintegrins for fibrinogen receptor, glycoprotein IIb-IIIa complex. also carboxyl-terminal 213-336) part 30% identity 1543-1656 von Willebrand factor remaining at end unique has cysteine-rich sequence. These results suggest portion structural similarities factor, may important synergistically stimulating activity NH2-terminal domain.