Kinetics of the neutral transition of human serum albumin

Abstract

The fast step in the conformational change of human serum albumin from the alkaline to the neutral form of the albumin-bilirubin complex is studied by various pH jump experiments in a stopped-flow apparatus. The results indicate that the fast step is caused by electrostatic attraction between a carboxylate group of bilirubin and a histidine residue of albumin.