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• W2030920142 endingPage "1926" @default.
• W2030920142 startingPage "1921" @default.
• W2030920142 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." @default.
• W2030920142 created "2016-06-24" @default.
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• W2030920142 date "1999-01-01" @default.
• W2030920142 modified "2023-09-25" @default.
• W2030920142 title "Polypeptide Compositions and NH₂-terminal Amino Acid Sequences of Proteins in Foxtail and Proso Millets" @default.
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• W2030920142 doi "https://doi.org/10.1271/bbb.63.1921" @default.
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