Cereal Chem 67:32-34   |  VIEW ARTICLE

Alpha- and Beta-Setarins: Methionine-Rich Proteins of Italian Millet (Setaria italica (L.) Beauv.).

A. P. Naren and T. K. Virupaksha. Copyright 1990 by the American Association of Cereal Chemists, Inc. 

Differential cryoprecipitation was employed for the purification of two methionine-rich proteins, alpha- setarin and beta-setarin from the alcohol-soluble prolamin fraction (setarin II) of Italian millet flour. Both alpha- and beta-setarins were low molecular weight polypeptides rich in sulfur amino acids. Methionine accounted for eight residues each out of a total of 63 and 71 amino acid residues in alpha- and beta-setarin, respectively. The peptide map pattern of cyanogen bromide cleaved alpha-setarin suggests that the methionine residues were randomly distributed throughout the polypeptide chain.