Oligo(methionyl) proteins
- 1 December 1984
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 145 (2) , 257-263
- https://doi.org/10.1111/j.1432-1033.1984.tb08546.x
Abstract
A number of model isopeptides containing oligo(methionine) chains varying in length (2–5 residues) covalently linked to the ɛ‐amino group of lysine were synthesized by solid‐phase procedures. Hydrolysis of these peptides by pepsin, chymotrypsin, cathepsin C (dipeptidyl peptidase IV) and intestinal aminopeptidase N was investigated using high‐performance liquid chromatography to identify and quantify the hydrolysis products. Methionine oligomers grafted onto lysine were cleaved to tripeptides by pepsin. Chymotrypsin preferentially hydrolyzed the methionyl‐methionine bond preceding the isopeptide bond. Cathepsin C released dimethionyl units from the covalently attached polymers. Intestinal aminopeptidase caused efficient hydrolysis of both peptides and isopeptide bonds although free methionine decreased the cleavage of the latter bond. Hydrophobic characteristics of oligo(methionine) chains promoted enzyme‐catalyzed transpeptidations resulting probably from acyl‐transfer‐type reactions. Complementary hydrolysis of the isopeptides by these digestive enzymes suggests that covalent attachment of oligo(amino acid)s to food proteins may improve their nutritional value.This publication has 30 references indexed in Scilit:
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