Interaction Between Guanine Hydrochloride and Bovine Serum Albumin

Mechanism of the interaction between guanine hydrochloride (GH) and bovine serum albumin (BSA) was studied by fluorospectrometry and UV-VIS spectrophotometry. Quenching of fluorescence of BSA was observed due to its reaction with GH, and the interaction was found to be a static quenching process. The binding constants, number of binding sites and types of binding force were found by applying the equation of site-binding model and thermodynamic equations. Synchronous fluorescence spectrometry was used in the study of the effect of GH on the configuration of BSA.