| pubmed-article:3604459 | pubmed:abstractText | The peptide fractions isolated from chymotryptic hydrolysates of wheat, rye and barley prolamines [this journal (1984) 178:173] were separated into pure peptides by high-performance liquid chromatography on octadecyl silica gel. The peptides which were most abundant were analyzed for amino acid composition and in part for amino acid sequence. Besides peptides which are typical for only one of the cereals investigated, peptides of similar composition were found in all three prolamines. These contain repeating sequences and are built up of mainly Gln (Q), Pro (P) and hydrophobic amino acids (X) such as Phe, Tyr, Ile, Val and Leu. One of the most frequent partial sequences is QQPQQPXP. | lld:pubmed |
