Collect. Czech. Chem. Commun.
1997, 62, 1815-1820
https://doi.org/10.1135/cccc19971815
Glycation of Human Serum Albumin by DL-Glyceraldehyde: A Fluorescence Quenching Study
Miroslav Štěpánek and Zdeněk Pavlíček
Department of Physical and Macromolecular Chemistry, Charles University, 128 40 Prague 2,Czech Republic
Abstract
Process of glycation of human serum albumin (HSA) by DL-glyceraldehyde was studied using steady-state and time-resolved fluorescence spectroscopy in the course of 100 h. During this period, measurements of steady-state tryptophan (Trp) and non-tryptophan (non-Trp) fluorescence of the glycated HSA were carried out, together with measurement of the non-Trp fluorescence decay and steady-state quenching using potassium iodide as a quencher. Observed changes in both Trp and non-Trp fluorescence intensity, as well as changes in non-Trp fluorescence lifetimes and quenching efficiency are explained with respect to a probable mechanism of glycation.
Keywords: Human serum albumin; Glycation; Fluorescence.
