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Despite great degree of similarity in the structure and conformation of different serum albumins, they often show marked difference in the ligand binding properties. These differences and similarities would be useful in understanding the molecular basis of ligand binding to serum albumins. In the present communication binding of bilirubin with sheep and bovine serum albumin have been studied by visible difference spectroscopy as a function of pH and ionic strength. The results suggest that the structure of bilirubin binding site in sheep serum albumin is similar to that in bovine serum albumin and that complex between sheep serum albumin and bilirubin is stabilized by electrostatic interactions. © 2019 Published by Innovative Publication.

Influence of pH and ionic strengths on bilirubin binding to sheep serum albumin