Simplified procedures for the isolation of HF3, bothropasin, disintegrin-like/cysteine-rich protein and a novel P-I metalloproteinase from Bothrops jararaca venom

Toxicon. 2009 Jun;53(7-8):797-801. doi: 10.1016/j.toxicon.2009.02.019. Epub 2009 Feb 28.

Abstract

HF3 and bothropasin are P-III hemorrhagic snake venom metalloproteinases (SVMPs) of Bothrops jararaca. The DC protein is composed of the disintegrin-like/cysteine-rich domains derived from the autolysis of P-III SVMPs. Here we describe simplified procedures for the isolation of HF3, bothropasin, the DC protein, and BJ-PI, a novel P-I SVMP. The isolated proteins were identified by mass spectrometry. BJ-PI is a potent caseinolytic enzyme devoid of hemorrhagic activity. HF3, bothropasin and BJ-PI show distinct fibrinogenolytic activities.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bothrops / physiology*
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Chromatography, Ion Exchange
  • Crotalid Venoms / isolation & purification*
  • Crotalid Venoms / toxicity
  • Electrophoresis, Polyacrylamide Gel
  • Hemorrhage / chemically induced
  • Hemorrhage / pathology
  • Metalloendopeptidases / isolation & purification*
  • Metalloendopeptidases / toxicity
  • Metalloproteases / isolation & purification*
  • Metalloproteases / toxicity
  • Mice
  • Molecular Sequence Data
  • Trypsin / chemistry
  • Viper Venoms / enzymology*

Substances

  • Crotalid Venoms
  • Viper Venoms
  • Metalloproteases
  • Trypsin
  • HF3 protein, Bothrops jararaca
  • Metalloendopeptidases
  • bothropasin, Bothrops jararaca