Abstract:
: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.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Brinegar AC,Peterson DMdoi
10.1104/pp.70.6.1767subject
Has Abstractpub_date
1982-12-01 00:00:00pages
1767-9issue
6eissn
0032-0889issn
1532-2548journal_volume
70pub_type
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