title: Wheat Inhibitors of Heterologous alpha-Amylases : Characterization of Major Components from the Monomeric Class.
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.
authors: Departmento de Bioquímica, E.T.S. Ingenieros Agrónomos, 28040 Madrid, Spain.
authors: L
authors: L
authors: Gomez
authors: R
authors: R
authors: Sanchez-Monge
authors: C
authors: C
authors: Lopez-Otín
authors: G
authors: G
authors: Salcedo