[Bilirubin binding to glycosylated human serum albumin].

Glycosylation of human blood serum albumin was carried out by means of prolonged incubation of the protein with an excess of D-glucose or D-glucose-6-phosphate. The amount of glucose covalently bound to the protein was determined using thiobarbituric acid or pyridoxal-5-phosphate. The binding of bilirubin to glycosylated albumin was decreased with an increase in amount of glucose incorporated into the macro-molecule.