Journal of Biochemistry Advance Access originally published online on April 11, 2007
Journal of Biochemistry 2007 141(6):827-833; doi:10.1093/jb/mvm096
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© 2007 The Japanese Biochemical Society.
Consequential Alterations in Haemoglobin Structure upon Glycation with Fructose: Prevention by Acetylsalicylic Acid
1School of Biology, University College of Science, University of Tehran; 2Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran; and 3International Graduate Research School of Molecular Basis of Dynamic Cellular Processes, Westfaelische Wilhelmes-Universitaet, Muenster, Germany
*To whom correspondence should be addressed. Tel: +98-21-6113214, Fax: +98-21-6640514, Email: 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 haemoglobin (Hb) to be glycated by fructose. Haemoglobin 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 sulphonate (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: fructation, glycation, Hb-AGE, HbA1c, haemoglobin, thioflavin T