Cereal Chem 58:83 - 85.  |  VIEW ARTICLE
Amino-Terminal Amino Acid Sequence of Hordein.

J. A. Bietz. Copyright 1981 by the American Association of Cereal Chemists, Inc. 

Hordein, the alcohol-soluble prolamin fraction from barley, was subjected to Edman degradation to investigate its N-terminal amino acid sequence. Although electrophoresis revealed whole hordein to be very heterogeneous, a single major sequence was obtained for 35-40 residues, demonstrating homology among many individual hordein polypeptides. This sequence was, in part, NH2-Arg-Gln-Leu-Asn-Pro-Ser-Ser- Gln-Glu-Leu-Gln-Ser-Pro-Gln-Gln- and represents primarily hordein's C components having molecular weights of approximately 53,000. Little sequence similarity was evident, however, between hordein and the prolamins from wheat or corn. These observations suggest that gene duplication followed by mutation is the most likely explanation for the occurrence of homologous prolamins in barley, as it is in other cereals.