| Literature DB >> 3579867 |
P I Payne, L M Holt, S M Reader, T E Miller.
Abstract
The proteins of Hordeum chilense grain were resolved into 25 major components by two-dimensional electrophoresis. Their solubilities in aqueous alcohol solutions were determined to distinguish prolamin storage proteins from metabolic and structural proteins. The prolamins were divided into two groups, based on the presence or absence of intermolecular disulfide bonds determined by gel-filtration chromatography. Using an incomplete set of Chinese Spring wheat-H. chilense disomic addition lines, the structural genes of 21 of the 26 most dominant seed proteins were assigned to chromosomes. The great majority of the prolamin genes, including those coding for a high molecular weight (HMW) prolamin subunit, was present on chromosome 1 Hch. However, a small number of prolamin genes also occurred on chromosomes 5 Hch and 7 Hch. A minor protein, probably belonging to the nonstorage group of proteins, is coded by genes on 5 Hch. Various ditelosomic addition lines and ditelosomic and disomic substitution lines for chromosome 7 Hch were also analyzed by electrophoresis. This technique revealed that the genes for three major prolamins occur on the beta arm of chromosome 7 Hch and that a gene for a minor protein, also thought to be a prolamin, occurs on the alpha arm. These results are discussed in relation to the evolution of prolamin genes in the Triticeae.Entities:
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Year: 1987 PMID: 3579867 DOI: 10.1007/bf00498951
Source DB: PubMed Journal: Biochem Genet ISSN: 0006-2928 Impact factor: 1.890