The post-translational proteolysis of the subunits of vicilin from pea (Pisum sativum L.).
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ABSTRACT: Tryptic-peptide profiles and amino acid sequencing of purified pea (Pisum sativum L.) vicilin subunits were used to show that their sequences were interrelated. Comparison with the nucleotide sequence of a cloned vicilin complementary DNA (mRNA) showed that all vicilin subunits could be derived from 50 000-Mr precursors containing up to two sites for post-translational proteolytic cleavage, and allowed these subunits to be located relative to the precursor.
SUBMITTER: Gatehouse JA
PROVIDER: S-EPMC1153911 | biostudies-other | 1982 Dec
REPOSITORIES: biostudies-other
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