Functional and sequence characterization of agkicetin, a new glycoprotein IB antagonist isolated from agkistrodon acutus venom

Yuh Ling Chen, Inn Ho Tsai

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61 Citations (Scopus)

Abstract

A new glycoprotein Ib (GPIb) antagonist, agkicetin, was purified from the venom of Agkistrodon acutus and characterized. It is a disulfide-linked heterodimer consisting subunits of 15 and 14 kDa. The subunits are homologous to each other and to other snake venom proteins of the C-type (Ca2+-dependent) lectin superfamily. Agkicetin behaved as a potent antagonist of von Willebrand Factor (vWF)-induced platelet agglutination (IC50=12.5 nM) and bound specifically to GPIb of fixed platelets with high affinity (Kd=38 nM). It did not bind coagulation factor IX and thrombin. Monoclonal antibody against epitope on the N-terminal domain of GPIb competed the binding of agkicetin with platelets. Reduced and alkylated agkicetin lost most of its inhibitory efficacy toward vWF-induced platelet agglutination.

Original languageEnglish
Pages (from-to)472-477
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume210
Issue number2
DOIs
Publication statusPublished - 1995 May 16

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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