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Rapid separation and analysis of N ϵ‐(γ‐glutamyl)‐ L ‐lysine‐and N ϵ‐(β‐aspartyl)‐ L ‐lysine in protein digests
Author(s) -
Otterburn Michael S.,
Sinclair William J.
Publication year - 1976
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740271114
Subject(s) - lysine , chemistry , chromatography , resolution (logic) , buffer (optical fiber) , glycine , ion exchange , amino acid , biochemistry , ion , organic chemistry , artificial intelligence , computer science , telecommunications
The separation and resolution of the isopeptides N ϵ(γ‐glutamyl)‐ L ‐lysine and N ϵ(β‐aspartyl)‐ L ‐lysine formed in heated proteins has been successfully achieved. The method demands a well‐characterised ion‐exchange column and the use of pH 3.40 lithium citrate buffer (0.2 N Li + ). Due to the variations in particle size and cross‐linkages in the ion‐exchange resin a computer‐assisted buffer gradient system has been developed. This system effects resolution of both isopeptides in 7 h. The use of leucyl‐glycine as an internal standard facilitates quantitative estimation of the isopeptides.