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Structural studies of the Maillard reaction products of a protein using ion trap mass spectrometry
Author(s) -
Tagami Uno,
Akashi Satoko,
Mizukoshi Toshimi,
Suzuki Eiichiro,
Hirayama Kazuo
Publication year - 2000
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/(sici)1096-9888(200002)35:2<131::aid-jms920>3.0.co;2-0
Subject(s) - maillard reaction , chemistry , amadori rearrangement , residue (chemistry) , lysozyme , sugar , d glucose , mass spectrometry , glycation , organic chemistry , chromatography , biochemistry , stereochemistry , receptor
The early stage products of the Maillard reaction of egg white lysozyme with D ‐glucose were studied. Incubation with D ‐glucose at 50°C for 20 days caused reaction on the Lys and Arg residues of lysozyme as follows: all of the six Lys residues and 10 of the 11 Arg residues in lysozyme reacted with D ‐glucose; Arg 61 did not react with D ‐glucose. The Lys residues reacted with D ‐glucose with 1 mol of dehydration per mole of residue, and the Arg residues reacted with 2 mol of dehydration per mole of residue. The major constituent of the Amadori product with the ϵ ‐amino group of the Lys residue and the D ‐glucose was found to be the β ‐pyranose form. The structure of the early stage product of the Maillard reaction of a protein with a sugar is the same as that of an amino acid with a sugar. Copyright © 2000 John Wiley & Sons, Ltd.