[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.

Keywords

Blood Glucose, Binding Sites, Glycosylation, Humans, Bilirubin, Spectrophotometry, Ultraviolet, In Vitro Techniques, Serum Albumin, Protein Binding

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