Purification and characterization of bitiscetin, a novel von Willebrand factor modulator protein from Bitis arietans snake venom

Jiharu Hamako, Taei Matsui, Masami Suzuki, Masayuki Ito, Kaori Makita, Yoshihiro Fujimura, Yasuhiro Ozeki, Koiti Titani

研究成果: Article査読

60 被引用数 (Scopus)

抄録

We have screened 20 snake venoms and purified a novel snake venom protein, named bitiscetin, from Bitis arietans venom that specifically binds to human von Willebrand factor (vWF) and induces platelet agglutination. Bitiscetin showed a heterodimeric structure composed of disulfide-linked α (16 kDa) and β (13 kDa) subunits on SDS-PAGE and showed a basic nature with pI value of 9.1, in contrast to botrocetin (pI 4.6), a vWF modulator isolated from another snake (Bothrops jararaca) venom. Bitiscetin-induced platelet agglutination was dependent on vWF and platelet membrane glycoprotein (GP) Ib, but not on Ca2+ and GPIIb/IIIa. vWF bound to bitiscetin but not to botrocetin electroblotted to a PVDF membrane after SDS-PAGE and this binding was diminished after reduction of disulfide bonds of bitiscetin. Bitiscetin did not cross-react to anti-botrocetin monoclonal antibodies. These results suggest that bitiscetin directly interacts with vWF and requires the protein conformation for its interaction as well as botrocetin, but its interaction manner with vWF appears to be different from that of botrocetin.

本文言語English
ページ(範囲)273-279
ページ数7
ジャーナルBiochemical and Biophysical Research Communications
226
1
DOI
出版ステータスPublished - 04-09-1996

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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