albumin - publications

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1. Rejuvenation Res. 2012 Apr;15(2):201-5.

Kinetics of advanced glycation end products formation on bovine serum albumin
with various reducing sugars and dicarbonyl compounds in equimolar ratios.

Luers L, Rysiewski K, Dumpitak C, Birkmann E.

1 Institut für Physikalische Biologie, Heinrich-Heine-Universität , Dusseldorf,
Germany .

Abstract Reducing sugars and reactive dicarbonyl compounds play a major role in
glycation of proteins in vivo. Glycation of proteins is the first step in of a
nonenzymatic reaction, resulting in advanced glycation end products (AGEs). AGEs
can inactivate proteins or modify their biological activities. Therefore, it is
important to understand the mechanism of AGE formation. Here, we systematically
analyzed the kinetics of AGE formation in vitro by fluorescence and absorption
measurements utilizing a microplate reader system and bovine serum albumin (BSA)
as a model protein. Comparing different concentrations of BSA, we applied various
reducing sugars and reactive dicarbonyl compounds as AGE-inducing agents at
different concentrations. In summary, this experimental setup enabled us to
measure the kinetics of AGE formation in an efficient and defined way.

PMID: 22533432 [PubMed - in process]