title: Polypeptide compositions and NH2-terminal amino acid sequences of proteins in foxtail and proso millets.
abstract: Seed protein of foxtail and proso millets were fractionated into polypeptides that were analyzed for their major protein, prolamin, and the NH2-terminal amino acid sequences 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 classified into two groups. The major polypeptides of 27-19 kDa were rich in leucine and alanine, whereas the 17-14 kDa polypeptides were rich in methionine and cysteine. Glutelin-like proteins that were extracted with a reducing reagent were high in proline content, the major polypeptides being 17 and 20 kDa. The NH2-terminal amino acid sequence showed that the major polypeptides of prolamin were homologous to alpha-zein and a glutelin-like protein containing the Pro-Pro-Pro sequence, like the repetitive sequence of gamma-zein. Although the prolamin consisted of a similar subunit to that of zein, polypeptides with various pI values were found among them.
authors.affiliation: Iwate Industrial Research Institute, Morioka, Japan. kohama@sv02.kiri.pref.iwate.jp
authors.forename: K
authors.initials: K
authors.lastname: Kohama
authors.forename: T
authors.initials: T
authors.lastname: Nagasawa
authors.forename: N
authors.initials: N
authors.lastname: Nishizawa
mesh_terms: D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D008970:Molecular Weight; D008897:Panicum / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D055315:Prolamins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D010446:Peptide Fragments; D010455:Peptides; D010940:Plant Proteins; D055315:Prolamins