Synthesis of Oat Globulin Precursors

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.