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ANALYTICAL CHARACTERIZATION OF THE PRODUCTS OF NONENZYMATIC GLYCOSYLATION OF LYSOZYME
Author(s) -
LESLIE R. B.,
HWANG S. H.,
TAKACS S. F.,
TREBILCOCKGUZMAN M.,
DAUN H.
Publication year - 1990
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1990.tb00847.x
Subject(s) - chemistry , glycosylation , amadori rearrangement , lysozyme , periodate , oxalic acid , maillard reaction , chromatography , biochemistry , hydrolysis , glycation , receptor
The quantitative analysis of the reaction products of the water activity dependent nonenzymatic glycosylation of lysozyme was not straightforward. Difficulties arose in the determination of the number of bound glucose molecules because glycosylation leads to glucose mediated protein aggregation, and the likely presence of a mixture of relatively labile Schiff‐base intermediates, and the more stable ketoamine products generated by Amadori rearrangement.Polyacrylamide gel electrophoresis was used to monitor protein aggregation; periodate oxidation, nuclear magnetic resonance (NMR), and oxalic acid hydrolysis combined with HPLC, emerged as the most promising methods to quantitate the degree of glycosylation. Possible interpretations are advanced to explain the apparent discrepancies in degree of glycosylation suggested by the different analytical methods evaluated.