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. 1983 May 15;212(2):427–432. doi: 10.1042/bj2120427

Sequence specificity of the post-translational proteolytic cleavage of vicilin, a seed storage protein of pea (Pisum sativum L.).

J A Gatehouse, G W Lycett, A J Delauney, R R Croy, D Boulter
PMCID: PMC1152063  PMID: 6309143

Abstract

Amino acid sequence data from vicilin of pea (Pisum sativum L.) were compared with predicted sequences from complementary DNA species. The sites of potential post-translational proteolytic cleavage of vicilin precursor polypeptides were located in polar regions of the polypeptide, at acidic or amide residues. Proteolysis did not take place in precursors containing a functionally distinct sequence: neutral residue-hydrophobic residue-basic residue at the cleavage site. Differences between the genomic sequences encoding vicilin thus specify proteolytic cleavage of vicilin precursor polypeptides.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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