Biochemical characterization of a new disintegrin, flavostatin, isolated from Trimeresurus flavoviridis venom.

@article{Kawasaki1996BiochemicalCO,
  title={Biochemical characterization of a new disintegrin, flavostatin, isolated from Trimeresurus flavoviridis venom.},
  author={Tomihisa Kawasaki and Yasushi Sakai and Yuta Taniuchi and Kazuo Sato and Kumiko Maruyama and Masaru Shimizu and Seiji Kaku and Shingo Yano and Osamu Inagaki and Ken-ichi Tomioka and Isao Yanagisawa and Tsuneo Takenaka},
  journal={Biochimie},
  year={1996},
  volume={78 4},
  pages={245-52}
}
We biochemically characterized a new disintegrin, flavostatin, isolated from Trimeresurus flavoviridis venom. Flavostatin inhibited ADP-, collagen-, and thrombin receptor agonist peptide-induced platelet aggregation in human platelet-rich plasma (IC50 range: 59 to 111 nM) and blocked the binding of biotinylated human fibrinogen to purified GPIIb/IIIa with an inhibitory potency 31,000-fold higher than that of Arg-Gly-Asp-Ser (RGDS). Flavostatin strongly inhibited high-shear-stress-induced… CONTINUE READING