Interaction between Isoprenaline Hydrochloride with BSA

Mechanism of interaction between bovine serum albumin (BSA)and isoprenaline hydrochloride (IH) was studied by fluorospectrometry and capillary zone electrophoresis. As shown by the results of fluorospectrometry, significant quenching of fluorescence of BSA was found by its reaction with IH, and as judging from the fluorescene quenching constants (Kq=2.53×1013L·mol-1·s-1) obtained by Stern-Volmer equation, fluorescence quenching of BSA by IH was attributed to static quenching. The binding constant and number of binding site were found to be 1.72×104L·mol-1 and 1 by applying the equation of site-binding mode respectively. It was shown by the results of capillary zone electrophoresis that: values of binding constant and number of binding site were found to be 4.07×104L·mol-1 and 1 respectively.