Purification and characterization of Cry1Ac toxin binding proteins from the brush border membrane of Helicoverpa armigera midgut

Curr Microbiol. 2005 Dec;51(6):367-71. doi: 10.1007/s00284-005-0051-9. Epub 2005 Oct 25.

Abstract

Several Cry1Ac binding proteins from midgut of Helicoverpa armigera were purified using toxin-affinity chromatography. Enzyme assays showed that the purified proteins had strong aminopeptidase activity. The N-terminal sequences confidently identified a 124-kDa binding protein as an aminopeptidase N (APN), and some similarity suggests that a 162-kDa binding protein may also be an APN. Two minor binding proteins were not characterized.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aminopeptidases / analysis
  • Aminopeptidases / isolation & purification
  • Animals
  • Bacterial Proteins
  • CD13 Antigens / genetics
  • Chromatography, Affinity
  • Digestive System / chemistry
  • Electrophoresis, Polyacrylamide Gel
  • Immunoblotting
  • Insect Proteins / isolation & purification*
  • Microvilli / chemistry*
  • Moths / chemistry*
  • Receptors, Cell Surface / isolation & purification*
  • Sequence Analysis, Protein
  • Sequence Homology, Amino Acid

Substances

  • Bacterial Proteins
  • Cry toxin receptors
  • Insect Proteins
  • Receptors, Cell Surface
  • Aminopeptidases
  • CD13 Antigens