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Synthesis of Oat Globulin Precursors
Author(s) -
A. Chris Brinegar,
David M. Peterson
Publication year - 1982
Publication title -
plant physiology
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.70.6.1767
Subject(s) - avena , cleavage (geology) , storage protein , legume , in vitro , disulfide bond , biochemistry , in vivo , chemistry , globulin , biology , botany , genetics , immunology , paleontology , fracture (geology) , gene
The oat (Avena sativa L.) seed globulin was found to be synthesized in vitro as 60,000 to 64,000 dalton precursors. In vivo protein labeling yielded polypeptides of 58,000 to 62,000 daltons, suggesting cleavage of signal sequences from the precursors. Further cleavage is apparently required to separate the alpha and beta polypeptide sequences which are known to form disulfide-linked 53,000 to 58,000 dalton species in the (alphabeta)(6) holoprotein. The data are discussed with respect to analogous synthesis and processing of some legume 11S storage proteins.

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