Kinetics of Advanced Glycation End Products Formation on Bovine Serum Albumin with Various Reducing Sugars and Dicarbonyl Compounds in Equimolar Ratios

被引:18
作者
Luers, Lars [1 ,2 ]
Rysiewski, Karolina [2 ]
Dumpitak, Christian [2 ]
Birkmann, Eva [1 ,2 ]
机构
[1] Forschungszentrum Julich, Inst Complex Syst ICS 6, D-52425 Julich, Germany
[2] Univ Dusseldorf, Inst Phys Biol, Dusseldorf, Germany
关键词
IN-VITRO; NONENZYMATIC GLYCATION; MAILLARD REACTION; SITE-SPECIFICITY; METHYLGLYOXAL; PROTEINS; IDENTIFICATION; FRUCTOSE; GLYOXAL; GLUCOSE;
D O I
10.1089/rej.2011.1284
中图分类号
R592 [老年病学]; C [社会科学总论];
学科分类号
03 ; 0303 ; 100203 ;
摘要
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.
引用
收藏
页码:201 / 205
页数:5
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