期刊
MAILLARD REACTION: RECENT ADVANCES IN FOOD AND BIOMEDICAL SCIENCES
卷 1126, 期 -, 页码 253-256出版社
BLACKWELL PUBLISHING
DOI: 10.1196/annals.1433.060
关键词
m-aminophenylboronic acid; ESI; glycation; MALDI; mass spectrometry
Glycation of peptides and proteins by D-glucose is a universal, nonenzymatic reaction with important implications for the pathogenesis and diagnosis of many diseases, including diabetes mellitus. Whereas some modification sites have been identified in serum albumin and hemoglobin, a general approach to map glycation sites for nonabundant proteins present in complex mixtures, such as serum, is still missing. Here, we describe a universal enrichment procedure for glycated peptides using boronic acid affinity chromatography in the first dimension followed by reversed-phase chromatography, coupled either online to electrospray ionization mass spectrometry (ESI-MS) or offline to matrix-assisted laser desorption/ionization (MALDI) MS. This two-dimensional approach was optimized for high recoveries and low cross reactivities. For bovine serum albumin, a total of 31 Amadori peptides were identified in a tryptic digest corresponding to 26 different glycation sites.
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