Amino acid sequence of a cardiotoxin-like basic polypeptide (CLBP) with low cytotoxic activity isolated from the venom of the Formosan cobra (Naja naja atra)

Biochem Int. 1985 Dec;11(6):795-802.

Abstract

A cardiotoxin-like basic polypeptide, designated as CLBP, was isolated from the venom of Naja naja atra by gel filtration on Sephadex G-50 followed by CM-cellulose chromatography. The cytotoxicity toward Yoshida sarcoma cells and lethal toxicity toward mice of CLBP were both one-order lower than those of cardiotoxins and cobrotoxin, respectively. CLBP is a single polypeptide consisting of 61 amino acid residues with four intramolecular disulfide linkages. The amino acid sequence of CLBP shows a high degree of homology with those of cardiotoxins from the same venom, but differs in the 19 to 23 positions.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cobra Cardiotoxin Proteins* / isolation & purification
  • Cobra Cardiotoxin Proteins* / toxicity
  • Elapid Venoms* / isolation & purification
  • Elapid Venoms* / toxicity
  • Lethal Dose 50
  • Mice
  • Peptide Fragments / analysis
  • Peptides / toxicity
  • Structure-Activity Relationship

Substances

  • Cobra Cardiotoxin Proteins
  • Elapid Venoms
  • Peptide Fragments
  • Peptides