Isolation of three hordeins

✍ Scribed by John A. D. Ewart

• Publisher: John Wiley and Sons
• Year: 1980
• Tongue: English
• Weight: 619 KB
• Volume: 31
• Category: Article
• ISSN: 0022-5142
• DOI: 10.1002/jsfa.2740311109

✦ Synopsis

Abstract

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.