TY  - JOUR
AU  - Luers, Lars
AU  - Rysiewski, K.
AU  - Dumpitak, Christian
AU  - Birkmann, Eva
TI  - Kinetics of Advanced Glycation End Products Formation on Bovine Serum Albumin with Various Reducing Sugars and Dicarbonyl Compounds in Equimolar Ratios
JO  - Rejuvenation research
VL  - 15
IS  - 2
SN  - 1094-5458
CY  - Larchmont, NY
PB  - Liebert
M1  - FZJ-2015-04384
SP  - 201 - 205
PY  - 2012
AB  - 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.
KW  - Carbohydrates (NLM Chemicals)
KW  - Glycosylation End Products, Advanced (NLM Chemicals)
KW  - Serum Albumin, Bovine (NLM Chemicals)
KW  - Fructose (NLM Chemicals)
KW  - Ribose (NLM Chemicals)
KW  - Arginine (NLM Chemicals)
KW  - Glucose (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:22533432
UR  - <Go to ISI:>//WOS:000303383600021
DO  - DOI:10.1089/rej.2011.1284
UR  - https://juser.fz-juelich.de/record/202095
ER  -