A dimeric inhibitor or insect alpha-amylase from barley. Cloning of the cDNA and identification of the protein

Eur J Biochem. 1988 Feb 15;172(1):129-34. doi: 10.1111/j.1432-1033.1988.tb13864.x.

Abstract

A cDNA clone, designated pUP-44, whose longest open reading frame codes for a protein that is homologous to the wheat alpha-amylase inhibitors, has been isolated from a library obtained from developing barley endosperm. The deduced sequence for the mature protein, which is 122 residues long, is preceded by a sequence of 30 residues which has the typical features of a signal peptide. A closely corresponding protein, designated BDAI-1, has been isolated from mature endosperm. BDAI-1 behaves as a dimer and inhibits the alpha-amylase from the insect Tenebrio molitor at concentrations that have no effect on salivary or pancreatic alpha-amylases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Chromatography, Gel
  • Cloning, Molecular*
  • DNA / analysis*
  • Edible Grain / enzymology*
  • Enzyme Inhibitors
  • Hordeum / enzymology*
  • Molecular Sequence Data
  • Plant Proteins / analysis*
  • Protein Biosynthesis
  • RNA, Messenger / analysis
  • Sequence Homology, Nucleic Acid
  • Tenebrio / enzymology
  • Triticum / enzymology
  • Trypsin Inhibitors / analysis
  • alpha-Amylases / antagonists & inhibitors*

Substances

  • Enzyme Inhibitors
  • Plant Proteins
  • RNA, Messenger
  • Trypsin Inhibitors
  • DNA
  • alpha-Amylases