Journal of Biochemistry Advance Access published online on April 11, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm096
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© 2007 The Japanese Biochemical Society
Consequential Alterations in Hemoglobin Structure upon Glycation with Fructose: Prevention by Acetylsalicylic Acid
a School of Biology, University College of Science, University of Tehran, Tehran, Iran
b Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
c International Graduate Research School of Molecular Basis of Dynamic Cellular Processes, Westfaelische Wilhelmes-Universitaet, Muenster, Germany
* Corresponding author: M. Habibi-Rezaei: School of Biology, University College of Science, University of Tehran, Tehran, Iran. Tel: +98-21-6113214, Fax: +98-21-6640514, E-mail: mhabibi{at}khayam.ut.ac.ir
Received March 15, 2007; Accepted March 19, 2007
| Abstract |
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Increased fructose concentration in erythrocytes of diabetic patients subject hemoglobin (Hb) to be glycated by fructose. Hemoglobin glycation results in early and advanced glycation end products which are known as HbA1c and Hb-AGE, respectively. In diabetics the Hb-AGE content raises and the mean parameter multiplication value (PMV) for Hb-AGE has been calculated at 6 against non-diabetics. We are emphasizing on fluorescence descriptive pairs especially of 370/440 nm (
ex/
em) and thioflavin T binding process to characterize short-term Hb-AGE formation upon glycation with fructose or fructation. Secondary structure elements were estimated after far-UV circular dichroism spectropolarimetery which reveals up to 11.3% ß-content attainment for 20 days incubated Hb with fructose which is concurred with enhanced hydrophobicity of the protein. The later is described through enhanced 1-anilino-8-naphthalene sulfonate (ANS) binding to fructated protein. The preventive effect of acetylsalicylic acid on glycation of methemoglobin and consequently, Hb-AGE formation also has been included.
Key Words: Hb-AGE, HbA1c, Hemoglobin, Fructation, Glycation, Thioflavin T