Relationship between bovine serum albumin structure and its chemical equilibria with hydrogen and 5-hydroxytryptamine ions.
From the analysis of titration curves with hydrogen and 5-HT ions, it was found that the electrostatic interaction parameter of protein macroion and the number sites of 5-HT fixing were smaller over an acid and base pH range as compared to their values at neutral pH. Our data were interpreted by the conformational changes which can be induced when BSA is exposed to denaturation by acid and alkali pH.
Relationship between bovine serum albumin structure and its chemical equilibria with hydrogen and 5-hydroxytryptamine ions. From the analysis of titration curves with hydrogen and 5-HT ions, it was found that the electrostatic interaction parameter of protein macroion and the number sites of 5-HT fixing were smaller over an acid and base pH range as compared to their values at neutral pH. Our data were interpreted by the conformational changes which can be induced when BSA is exposed to denaturation by acid and alkali pH.