Journal Article

FZJ-2015-04384

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png 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. (Corresponding Author)FZJ*

2012
Liebert Larchmont, NY

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Please use a persistent id in citations: doi:10.1089/rej.2011.1284

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.

Keyword(s): Carbohydrates ; Glycosylation End Products, Advanced ; Serum Albumin, Bovine ; Fructose ; Ribose ; Arginine ; Glucose

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 452 - Structural Biology (POF2-452) (POF2-452)

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Database coverage:
; Current Contents - Clinical Medicine ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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