GLYCATION OF HUMAN SERUM-ALBUMIN BY DL-GLYCERALDEHYDE - A FLUORESCENCE QUENCHING STUDY

Process of glycation of human serum albumin (HSA) by DL-glyceraldehyde was studied using steady-state and time-resolved fluorescence spectro scopy in the course of 100 h. During this period, measurements of stea dy-state tryptophan (Trp) and non-tryptophan (non-Trp) fluorescence of the glycated HSA were carried out, together with measurement of the n on-Trp fluorescence decay and steady-state quenching using potassium i odide as a quencher. Observed changes in both Trp and non-Trp fluoresc ence intensity, as well as changes in non-Trp fluorescence lifetimes a nd quenching efficiency are explained with respect to a probable mecha nism of glycation.