The enzymatic activities and lethal toxins of Trimeresurus wagleri (speckled pit viper) venom

Toxicon. 1989;27(3):349-57. doi: 10.1016/0041-0101(89)90182-7.

Abstract

Trimeresurus wagleri (speckled pit viper) venom exhibited the usual set of enzyme activities occurring in pit viper venoms but the content of alkaline phosphomonoesterase was unusually high, whereas the proportions of protease and arginine ester hydrolase were very low. The venom also exhibited weak thrombin-like activity but did not exhibit hemorrhagic or anticoagulant activity. Analysis of the Sephadex G-200 gel filtration fractions of the venom indicated that the lethal fraction was a low mol.wt protein, and that fractions exhibiting phosphodiesterase, phosphomonoesterase, arginine ester hydrolase, thrombin-like enzyme, L-amino acid oxidase and phospholipase A activities were not lethal. Two lethal toxins, designated as wagleri toxins 1 and 2, were isolated from the venom using Sephadex G-50 gel filtration chromatography followed by SP-Sephadex C-25 ion exchange chromatography. The mol.wts of the two toxins were 8900 by gel filtration. The LD50 (i.v.) values in mice for wagleri toxins 1 and 2 are 0.17 microgram/g and 0.19 microgram/g, respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chickens
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Crotalid Venoms / analysis*
  • Crotalid Venoms / toxicity
  • Enzymes / analysis
  • Enzymes / isolation & purification
  • Hemorrhage / chemically induced
  • In Vitro Techniques
  • Lethal Dose 50
  • Male
  • Mice
  • Molecular Weight
  • Muscles / drug effects
  • Phosphoric Diester Hydrolases / isolation & purification
  • Rabbits
  • Thrombin / analysis
  • Toxins, Biological / isolation & purification
  • Toxins, Biological / toxicity
  • Whole Blood Coagulation Time

Substances

  • Crotalid Venoms
  • Enzymes
  • Toxins, Biological
  • Phosphoric Diester Hydrolases
  • Thrombin