Proso Millets Amino Acid Sequences

Seed protein of foxtai1 and proso millets were fractionated into polypeptides that were analyzed for their major protein, prolamin, and the NHrterminal amine acid seqllenccs of the proteins were determined. The proteins extracted from foxtail and proso millets were 64.1% and 80.0% prolamin, respectively. The polypeptides of the prolamins were classMed into two groups. The majer polypeptides of 27-19 kDa were rich in leucine and alanille, whereas the 17-14 kDa polypeptides were rich in methionine and cysteine. Gllltelin-like preteins that were extracted with a reducing reagent were high in preline content, the major pelypeptides being 17 and 20 kDa. The NH2-terrninal amino acid sequence showed tha"he major polypeptides of prolamin were homologolls to crzein and a glutelin-like protein containing the Pro-Pro-Pro sequence, like the repetitiye seqllence of 7-zein. Although the prelamin consisted of a similar subunit to that of zein, polypeptides with various pl yalues were found ameng them.