Journal
ANALYTICA CHIMICA ACTA
Volume 617, Issue 1-2, Pages 85-96Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.aca.2007.12.027
Keywords
glycation; mass spectrometry; N-epsilon-carboxymethyllysine; N-epsilon-fructoselysine; pyrraline; dairy products
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Free and protein-bound forms of early and advanced glycation-induced lysine (Lys) modifications were quantified in dairy products by LC-MS/MS using a stable isotope dilution assay. The glycation profiles for N-epsilon-fructoselysine (FL), N-epsilon-carboxymethyllysine (CML) and pyrraline (Pyr) were monitored in raw and processed cow milk to investigate whether free glycation products could serve as fast and simple markers to assess the extent of protein glycation in dairy products. In all milk samples, the fraction of free glycation adducts was predominantly composed of advanced modifications, e.g. 8.34 +/- 3.81 nmol CML per mu mol of free Lys (Lys(free)) and 81.5 +/- 87.8 nmol Pyr mu mol(-1) Lys(free)(-1) vs. 3.72 +/- 1.29 nmol FL mu mol(-1) Lys(free)(-1). In contrast, the protein-bound early glycation product FL considerably outweighed the content of CML and Pyr in milk proteins of raw and processed cow milk, whereas severely heat treated milk products, e.g. condensed milk, contained a higher amount of protein-bound advanced glycation adducts. Typical values recorded for milk samples processed under mild conditions were 0.47 +/- 0.08 nmol FL mu mol(-1) of protein-bound Lys (Lys(p-b)), 0.04 +/- 0.03 nmol CML mu mol(-1) Lys(p-b)(-1) and 0.06 +/- 0.02 nmol Pyr mu mol(-1) Lys(p-b)(-1). It was particularly noticeable, however, that mild heat treatment of raw milk, i.e. pasteurization and UHT treatment, did not significantly increase the amount of both free and protein-bound Lys modifications. In conclusion, the profiles of free and protein-bound glycation-induced Lys modifications were found to be different and a screening of free glycation adducts does, therefore, not allow for a conclusion about the protein glycation status of dairy products. (C) 2008 Elsevier B.V. All rights reserved.
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