Comparison of modification sites formed on human serum albumin at various stages of glycation.

ABSTRACT:

Background

Many of the complications encountered during diabetes can be linked to the non-enzymatic glycation of proteins, including human serum albumin (HSA). However, there is little information regarding how the glycation pattern of HSA changes as the total extent of glycation is varied. The goal of this study was to identify and conduct a semi-quantitative comparison of the glycation products on HSA that are produced in the presence of various levels of glycation.

Methods

Three glycated HSA samples were prepared in vitro by incubating physiological concentrations of HSA with 15 mmol/l glucose for 2 or 5 weeks, or with 30 mmol/l glucose for 4 weeks. These samples were then digested and examined by matrix-assisted laser desorption/ionization time-of-flight mass spectrometr

SUBMITTER: Barnaby OS 

PROVIDER: S-EPMC3053033 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature