Kinetics of neutral transition of human serum albumin.
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 first step is caused by electrostatic attraction between a carboxylate group of bilirubin and a histidine residue of albumin.
D001663:Bilirubin / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011487:Protein Conformation; D012709:Serum Albumin / Q000378:metabolism*; D013057:Spectrum Analysis
D012709:Serum Albumin; D001663:Bilirubin