QUANTITATIVE ANALYSIS OF GLYCATION PATTERNS IN HUMAN SERUM ALBUMIN USING 16O/18O-LABELING AND MALDI-TOF MS

摘要

BackgroundThe glycation of human serum albumin (HSA) during diabetes can affect the ability of this protein to bind drugs and small solutes in blood. This study describes the use of ¹⁶O/¹⁸O-labeling and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry to compare the levels of modification that occur throughout HSA under various glycation conditions in vitro. These quantitative studies build on a recent report that has identified the early and advanced glycation products that are formed on such samples of HSA.