Thrombin-like activity in snake venoms from Peruvian Bothrops and Lachesis genera

Toxicon. 1991;29(9):1151-4. doi: 10.1016/0041-0101(91)90212-a.

Abstract

Venoms from Lachesis muta muta, Bothrops pictus, B. barnetti, B. atrox and B. hyoprorus coagulate in vitro canine fibrinogen, and both bovine fibrinogen and bovine plasma. B. barnetti and L. muta muta venoms have greater activity on canine fibrinogen and B. atrox and B. hyoprorus venoms, a greater activity on bovine fibrinogen. Gel filtration showed one peak of coagulant activity in all venoms except B. atrox venom which possessed two peaks. The apparent mol. wt of these enzymes ranged from 45,000 to 69,000.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blood Coagulation / drug effects*
  • Cattle
  • Chemical Fractionation
  • Chromatography, Gel
  • Crotalid Venoms / chemistry
  • Crotalid Venoms / toxicity*
  • Dogs
  • Fibrinogen / metabolism*
  • Molecular Weight
  • Thrombin / metabolism

Substances

  • Crotalid Venoms
  • Fibrinogen
  • Thrombin