Quantitative analysis of glycation sites on human serum albumin using (16)O/(18)O-labeling and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.

ABSTRACT:

Background

One of the long term complications of diabetes is the non-enzymatic addition of glucose to proteins in blood, such as human serum albumin (HSA), which leads to the formation of an Amadori product and advanced glycation end products (AGEs). This study uses (16)O/(18)O-labeling and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) to provide quantitative data on the extent of modification that occurs in the presence of glucose at various regions in the structure of minimally glycated HSA.

Methods

Normal HSA, with no significant levels of glycation, was digested by various proteolytic enzymes in the presence of water, while a similar sample containing in vitro glycated HSA was digested in (18)O-enriched water. These samples w

SUBMITTER: Barnaby OS 

PROVIDER: S-EPMC2883623 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature