Purification and characterization of a paralytic polypeptide from larvae of Myrmeleon bore

Biochem Biophys Res Commun. 1995 Oct 4;215(1):167-71. doi: 10.1006/bbrc.1995.2448.

Abstract

A toxic substance was purified from larvae of the antilion, Myrmeleon bore, by DEAE Sephacel and Phenyl Superose column chromatography. The substance was a large polypeptide with a molecular weight of about 165-167 kDa. Its paralytic activity measured by injection against German cockroaches was about 130 times higher than that of tetrodotoxin on a molar basis.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arthropod Venoms / chemistry
  • Arthropod Venoms / isolation & purification*
  • Arthropod Venoms / pharmacology
  • Cockroaches / drug effects
  • Insecta*
  • Larva / metabolism
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Fragments / chemistry
  • Peptides / chemistry
  • Peptides / isolation & purification*
  • Peptides / pharmacology
  • Tetrodotoxin / pharmacology
  • Toxins, Biological / chemistry
  • Toxins, Biological / isolation & purification*
  • Toxins, Biological / pharmacology
  • Venoms / chemistry*

Substances

  • Arthropod Venoms
  • Peptide Fragments
  • Peptides
  • Toxins, Biological
  • Venoms
  • Tetrodotoxin