The post-translational proteolysis of the subunits of vicilin from pea (Pisum sativum L.).
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.
D000595:Amino Acid Sequence; D007887:Fabaceae / Q000378:metabolism*; D008954:Models, Biological; D010446:Peptide Fragments / Q000032:analysis; D010940:Plant Proteins; D014674:Plant Proteins, Dietary / Q000378:metabolism*; D010946:Plants, Medicinal; D011499:Protein Processing, Post-Translational; D055314:Seed Storage Proteins
D010446:Peptide Fragments; D010940:Plant Proteins; D014674:Plant Proteins, Dietary; D055314:Seed Storage Proteins; C015575:vicilin protein, plant