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. 1982 Dec 1;207(3):629-32.
doi: 10.1042/bj2070629.

The post-translational proteolysis of the subunits of vicilin from pea (Pisum sativum L.)

J A Gatehouse, G W Lycett, R R Croy, D Boulter

The post-translational proteolysis of the subunits of vicilin from pea (Pisum sativum L.)

J A Gatehouse et al. Biochem J. .

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.

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