Authors : Mohammad Najmuddin Khan, Mohammad Najmuddin Khan
DOI : 10.18231/j.ijcbr.2019.058
Volume : 6
Issue : 3
Year : 2019
Page No : 259-262
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.
Keywords: Sheep serum albumin, Bovine serum albumin, Bilirubin binding, ionic strength, pH.