[Thermochemical studies on the reaction of barbital sodium with bovine serum albumin].

The mechanism of interaction mechanism of barbital sodium with bovine serum albumin (BSA) was studied by fluorescence spectroscopy. According to the thermodynamics parameters, the main sort of binding force of the interaction is electrostatic force, and binding BBTS to BSA is a spontaneous supermolecular interaction in which entropy increases and Gibbs free energy decrease. The formation constants of them were analyzed according to Stern-Volmer equation and double-reciprocal equation, and are smaller at high temperature than at low temperature. It is confirmed that the combination reaction of BBTS with BSA is a static quenching process. The change in the micro-circumstance of amino of bovine serum albumin was analyzed by synchronous fluorescence spectrometry.