| Literature DB >> 24247781 |
R Sanchez-Monge1, D Barber, E Mendez, F García-Olmedo, G Salcedo.
Abstract
Three α-amylase inhibitors, designated Inh. I, II and III have been purified from the 70% ethanol extract of hexaploid wheat (Triticum aestivum L.) and characterized by amino acid analysis, N-terminal amino acid sequencing and enzyme inhibition tests. Inhibitors I and III have identical N-terminal sequences and inhibitory properties to those of the previously described 0.19/0.53 group of dimeric inhibitors. Inhibitor II has an N-terminal sequence which is identical to that of the previously described 0.28 monomeric inhibitor, but differs from it in that in addition to being active against α-amylase from Tenebrio molitor, it is also active against mammalian salivary and pancreatic α-amylases. Compensating nulli-tetrasomic and ditelosomic lines of wheat cv. 'Chinese Spring' have been analysed by two-dimensional electrophoresis, under conditions in which there is no overlap of the inhibitors with other proteins, and the chromosomal locations of the genes encoding these inhibitors have been established: genes for Inh. I and Inh. III are in the short arms of chromosomes 3B and 3D, respectively, and that for Inh. II in the short arm of chromosome 6D.Entities:
Year: 1986 PMID: 24247781 DOI: 10.1007/BF00261464
Source DB: PubMed Journal: Theor Appl Genet ISSN: 0040-5752 Impact factor: 5.699