Abstract
This review is written to evaluate the possible utility of thermal measurement in the interaction study of drug with serum albumin. DSC measurement showed that species difference exist with respect to the conformational stability and the mechanism of unfolding pathway for mammalian albumin. In addition, the existence of three binding sites on human serum albumin molecule was confirmed from flow microcalorimetry. Moreover, the chemical and biological stability of oxidized albumin was mentioned. This discussion will be useful in the development of knowledge about structure and function of biopolymers including serum albumin.
