Characterization of advanced glycation end products for biochemical studies: side chain modifications and fluorescence characteristics
Schmitt, Annett, Schmitt, Johannes, Münch, Gerald, and Gasic-Milencovic, Jovana (2005) Characterization of advanced glycation end products for biochemical studies: side chain modifications and fluorescence characteristics. Analytical Biochemistry, 338 (2). pp. 201-215.
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Advanced glycation end products (AGEs) are known to be involved in the pathogenesis of several diseases and therefore effects of AGEs on cells are the objective of numerous investigations. Since AGEs used in biochemical studies are usually not chemically characterized, comparison of data is difficult if not impossible. To find a suitable characterization protocol, human serum albumin was reacted with different concentrations of glucose, methyl glyoxal, and glyoxylic acid. The obtained AGEs were characterized with respect to the extent of side chain modifications (lysine and arginine), the carboxymethyl lysine and carbonyl content, and the fibrillar state. Additionally, their fluorescence and absorbance characteristics were extensively studied. Although we found significant differences in the degree of modification and in AGE-specific fluorescence when using different modifiers, the results provide important information and allow comparing AGEs derived from different modifier concentrations. The results also suggest strong conformational changes within the modified proteins. In the present paper we propose a set of parameters that is sufficient to partially characterize AGEs used for biochemical studies.
|Item Type:||Article (Refereed Research - C1)|
|Keywords:||advanced glycation end products; aging/gerontology; AGE characterization; fluorescence; side chain modifications|
|FoR Codes:||11 MEDICAL AND HEALTH SCIENCES > 1109 Neurosciences @ 100%|
|SEO Codes:||92 HEALTH > 9201 Clinical Health (Organs, Diseases and Abnormal Conditions) > 920111 Nervous System and Disorders @ 100%|
|Deposited On:||12 Jun 2009 12:48|
|Last Modified:||18 Oct 2013 00:37|
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