Comparative investigations of partial amino acid sequences of prolamins and glutelins from cereals. VIII. Amino acid sequences of glutelin peptides

Abstract

The peptide fractions isolated from chymotryptic hydrolysates of wheat, rye and barley glutelins were separated by high-performance liquid chromatography on octadecyl silica gel. The peptides obtained were analysed for their amino acid composition and some also for their amino acid sequence. Characteristic sequences of peptides from wheat glutelin can be grouped into three types. The first type contains a high amount of Gly and frequently Tyr in the N-terminal positions. A typical partial sequence, which occurs repeated in two peptides, is QGQQPGQGQ. Sequences of this type are found in high-molecular-weight subunits. The second type is characterized by the sequence SQn (n = 3-5) followed by a hydrophobic tripeptide e.g., PPF, PVL; the most frequent sequence is SQQQQPPF. Low-molecular-weight subunits contain sequences of this type. The third type, which has partial sequences such as QQPQQPFP, corresponds to typical peptides from prolamin. Most sequences of peptides from rye and barley glutelins can be divided into two groups. The predominant type shows prolamin-like sequences, e.g., PQQPXPQQ with X being F or I. The second type is similar to glycine-rich peptides from wheat glutelin, except that repeating sequences are less frequent.