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Molecules 2014, 19(4), 4880-4896; doi:10.3390/molecules19044880

Kinetics of Glycoxidation of Bovine Serum Albumin by Methylglyoxal and Glyoxal and its Prevention by Various Compounds

1,* , 1 and 1,2
1 Department of Biochemistry and Cell Biology, University of Rzeszów, Zelwerowicza St. 4, PL 35-601 Rzeszów, Poland 2 Department of Molecular Biophysics, University of Łódź, Pomorska 141/143, 90-236 Łódź, Poland
* Author to whom correspondence should be addressed.
Received: 19 February 2014 / Revised: 9 March 2014 / Accepted: 10 March 2014 / Published: 17 April 2014
(This article belongs to the Section Medicinal Chemistry)
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The aim of this study was to compare several methods for measurement of bovine serum albumin (BSA) modification by glycoxidation with reactive dicarbonyl compounds (methylglyoxal ‒ MGO and glyoxal ‒ GO), for studies of the kinetics of this process and to compare the effects of 19 selected compounds on BSA glycation by the aldehydes. The results confirm the higher reactivity of MGO with respect to GO and point to the usefulness of AGE, dityrosine and N′-formylkynurenine fluorescence for monitoring glycation and evaluation of protection against glycation. Different extent of protection against glycation induced by MGO and GO was found for many compounds, probably reflecting effects on various stages of the glycation process. Polyphenols (genistein, naringin and ellagic acid) were found to protect against aldehyde-induced glycation; 1-cyano-4-hydroxycinnamic acid was also an effective protector.
Keywords: glycation; kinetics; methylglyoxal; glyoxal; antioxidants glycation; kinetics; methylglyoxal; glyoxal; antioxidants
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Sadowska-Bartosz, I.; Galiniak, S.; Bartosz, G. Kinetics of Glycoxidation of Bovine Serum Albumin by Methylglyoxal and Glyoxal and its Prevention by Various Compounds. Molecules 2014, 19, 4880-4896.

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