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Isolation of three hordeins
Author(s) -
Ewart John A. D.
Publication year - 1980
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740311109
Subject(s) - molecular mass , amino acid residue , residue (chemistry) , chemistry , amino acid , lysine , electrophoresis , polypeptide chain , biochemistry , peptide sequence , enzyme , gene
Three major barley prolamins of high, and nearly equal, electrophoretic mobilities have been separated and analysed. They appear to be free from SH groups and to have single polypeptide chains. The amino acid composition is broadly similar to those of wheat gliadins but the barley proteins have more Pro, Lys, Gly and Val, and less Asx. The molecular weights of the fast, middle, and slow members of the group are 43, 44 and 43 × 10 3 , respectively. The relative mobilities stem from the presence of an extra Arg residue in the two faster proteins, while the dissimilar speeds within this pair are accounted for by inequality of molecular size.