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@ARTICLE{Luers:202095,
author = {Luers, Lars and Rysiewski, K. and Dumpitak, Christian and
Birkmann, Eva},
title = {{K}inetics of {A}dvanced {G}lycation {E}nd {P}roducts
{F}ormation on {B}ovine {S}erum {A}lbumin with {V}arious
{R}educing {S}ugars and {D}icarbonyl {C}ompounds in
{E}quimolar {R}atios},
journal = {Rejuvenation research},
volume = {15},
number = {2},
issn = {1094-5458},
address = {Larchmont, NY},
publisher = {Liebert},
reportid = {FZJ-2015-04384},
pages = {201 - 205},
year = {2012},
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.},
keywords = {Carbohydrates (NLM Chemicals) / Glycosylation End Products,
Advanced (NLM Chemicals) / Serum Albumin, Bovine (NLM
Chemicals) / Fructose (NLM Chemicals) / Ribose (NLM
Chemicals) / Arginine (NLM Chemicals) / Glucose (NLM
Chemicals)},
cin = {ICS-6},
ddc = {610},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {452 - Structural Biology (POF2-452)},
pid = {G:(DE-HGF)POF2-452},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:22533432},
UT = {WOS:000303383600021},
doi = {10.1089/rej.2011.1284},
url = {https://juser.fz-juelich.de/record/202095},
}