Proteolytic specificity of rhodostoxin, the major hemorrhagin of Calloselasma rhodostoma (Malayan pit viper) venom

Toxicon. 1997 Jun;35(6):979-84. doi: 10.1016/s0041-0101(96)00186-9.

Abstract

The proteolytic specificity of rhodostoxin, the major hemorrhagin from Calloselasma rhodostoma (Malayan pit viper) venom was investigated using oxidized B-chain of bovine insulin as substrate. Six peptide bonds were cleaved: Ser9-Hist10, His10-Leu11, Ala14-Leu15, Tyr16-Leu17, Gly20-Glu21 and Phe24-Phe25. Deglycosylated rhodostoxin, however, cleaved primarily at Arg22-Gly23.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crotalid Venoms / metabolism*
  • Glycoproteins / metabolism*
  • Hemorrhage / chemically induced*
  • Hydrolysis
  • Metalloendopeptidases / metabolism*
  • Mice
  • Molecular Sequence Data
  • Substrate Specificity

Substances

  • Crotalid Venoms
  • Glycoproteins
  • rhodostoxin protein, Calloselasma rhodostoma
  • Metalloendopeptidases