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Model Studies on Protein Glycation
Author(s) -
Schwarzenbolz Uwe,
Mende Susann,
Henle Thomas
Publication year - 2008
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1433.021
Subject(s) - glyoxal , chemistry , cysteine , lysine , derivatization , arginine , glycation , maillard reaction , nucleophile , casein , reactivity (psychology) , amino acid , biochemistry , chromatography , organic chemistry , high performance liquid chromatography , enzyme , medicine , receptor , alternative medicine , pathology , catalysis
Mixtures of N α ‐hippurylarginin, N α ‐hippuryllysine, and glyoxal were incubated in the absence and presence of N α ‐acetylcysteine in order to assess the individual reactivity of these nucleophilic amino acid residues. The incubations were performed under atmospheric and high hydrostatic pressure (400 MPa), and, at the same time, β‐casein was reacted with glyoxal. The results showed that arginine is the main partner for glyoxal in the absence of cysteine, whereas a lysine derivatization was not apparent. In the presence of cysteine, however, arginine was almost completely protected from the reaction, whereas a noticeable formation of lysine derivatives, mainly carboxymethyllysine, was observed. Based on these findings, a reaction mechanism is proposed to explain the influence of cysteine on the reaction.