These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Wheat Inhibitors of Heterologous alpha-Amylases : Characterization of Major Components from the Monomeric Class.
    Author: Gomez L, Sanchez-Monge R, Lopez-Otín C, Salcedo G.
    Journal: Plant Physiol; 1991 Jul; 96(3):768-74. PubMed ID: 16668253.
    Abstract:
    The four major components of the wheat monomeric alpha-amylase inhibitors (WMAI) from wheat, Triticum aestivum, endosperm have been isolated and characterized. Two of them, WMAI-1 and WMAI-2, are highly active against the alpha-amylase from the insect Tenebrio molitor and their N-terminal amino acid sequences indicate that they are closely related to each other (86% identical residues) and to the other members of the family (subunits of dimeric and tetrameric alpha-amylase inhibitors and trypsin inhibitors). WMAI-1, which is identical to the previously described 0.28 inhibitor, is encoded by a gene located in the short arm of chromosome 6D and WMAI-2 by a gene in the short arm of chromosome 6B. Components 3 and 4, which have blocked N-terminal residues, have identical internal amino acid sequences and are a separate class of proteins with respect to WMAI-1 and WMAI-2, although their amino acid composition and apparent molecular weights are quite similar. Their inhibitory activity versus alpha-amylases is either unstable during the purification process or due to contamination with other inhibitors.
    [Abstract] [Full Text] [Related] [New Search]