Collect. Czech. Chem. Commun. 1997, 62, 1650-1662

Chemiluminescence of Glycated Human Serum Albumin: Comparison with Synthetic Polymer

Robert Zoulíka, Zdeněk Pavlíčeka, Richard Tykvab and Antonín Šenfelda

a Department of Physical and Macromolecular Chemistry, Charles University, 128 40 Prague 2, Czech Republic
b Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 166 10 Prague 6, Czech Republic


The mechanism of protein glycation (nonenzymatic glycosylation) is complicated by existence of a variety of factors which affect both the kinetics and specificity of protein modification. In order to eliminate some of these factors, we have used a synthetic copolymer on the basis of polymethacrylic acid amide. Human serum albumin and the copolymer were incubated with glycolaldehyde for a period up to 168 h. The products of glycation were oxidized by atmospheric oxygen in the presence of horse-radish peroxidase leading to species in electronically excited states. The behaviour of human serum albumin and synthetic copolymer during glycation was compared on the basis of chemiluminescent data. In both cases, the chemiluminescence curves had biphasic character. On this experimental basis, a scheme was proposed for the glycation mechanism.

Keywords: Protein glycation; Mechanism; Chemiluminescence; Human serum albumin.