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• W2058055099 abstract "We have isolated cDNA clones for an alcohol-soluble prolamin from oat. A complete eDNA clone has been sequenced and the corresponding amino-acid sequence deduced. The cDNA clone shows the presence of a 28 amino acid signal peptide that is cleaved at an unusual Tyr↓Glu cleavage site. N-terminal sequencing of the first 19 amino acids of the mature 16 kDa protein verifies this site as the site of cleavage as well as confirming the identity of the protein encoded for by this cDNA. The protein is rich in sulphur-containing amino acids, and does not have a typical repeated amino acid sequence arrangement that has been seen in some classes of prolamins from other cereals. An interesting feature of this clone is that it contains in the 3'- end of the clone regions of near-exact homology with sequences found at the 3'-end of a (DNA clone for the major salt-soluble oat globulin protein. These results are discussed in regards to regulation of protein content and packaging in cereal endosperm tissue." @default.
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• W2058055099 date "1988-01-01" @default.
• W2058055099 modified "2023-09-26" @default.
• W2058055099 title "The Nucleotide Sequence of a cDNA for a Major Prolamin (Avenin) in Oat (Avena saliva L. cultivar Hinoat) which Reveals Homology with Oat Globulin" @default.
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• W2058055099 doi "https://doi.org/10.1016/s0015-3796(88)80089-1" @default.
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