Comparison of in vitro protein modification withadvanced glycation endproduct (AGE) precursorsmethylglyoxal, glyoxal, 3-deoxyglucosone andglucose using mass spectrometry

摘要

Purified lysozyme was incubated with purified dicarbonyls or glucose in phosphate buffer, pH 7.4, with incubation solutions replenished every 2 or 3 days. Electrospray mass spectrometry analysis of the products revealed that methylglyoxal (MG) and glyoxal (G) are more reactive than 3-DG, while glucose is less reactive by several orders of magnitude.