Characterization of a novel legumin alpha-amylase inhibitor from chickpea (Cicer arietinum L.) seeds

Biosci Biotechnol Biochem. 2009 May;73(5):1200-2. doi: 10.1271/bbb.80776. Epub 2009 May 7.

Abstract

A proteinaceous alpha-amylase inhibitor (CLAI) was purified from Cicer arietinum seeds. It had a molecular mass of 25.947 kDa and inhibited alpha-amylases from plants and mammals. Analysis of the amino acid sequence of a polypeptide from CLAI showed that it was different from other known alpha-amylase inhibitors, but had high identity to legumins from Cicer arietinum (100%) and Vicia faba var. minor (90%).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chromatography, Liquid
  • Cicer / chemistry*
  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / isolation & purification
  • Enzyme Inhibitors / pharmacology*
  • Humans
  • Legumins
  • Molecular Sequence Data
  • Plant Proteins / chemistry
  • Plant Proteins / isolation & purification
  • Plant Proteins / pharmacology*
  • Seeds / chemistry*
  • alpha-Amylases / antagonists & inhibitors*

Substances

  • Enzyme Inhibitors
  • Plant Proteins
  • alpha-Amylases