[Microcalorimetric study of the parameters of dicloxacillin binding with human serum albumin at different temperatures].

The thermodynamic parameters of human serum albumin (HSA) binding with dicloxacillin, an antibiotic widely used in clinical practice, were determined with the method of differential flow microcalorimetry at 18, 25, 30, 37 and 45 degrees C. The experiments were performed at two ionic strengths: 0.02 and 0.

[Microcalorimetric study of the effect of temperature on methicillin binding with human serum albumin].

The curves of the calorimetric titration of human serum albumin (HSA) with methicillin at different temperatures were plotted. Unlike the widely used serial continuous flow calorimeters, the presented modification of a differential continuous flow microcalorimeter provided its application at wider temperature ranges and higher sensitivity. The possibility of obtaining equilibrium characteristics of the complexing at diverse temperatures, including the temperature of 37 degrees C allowed a more profound investigation of the molecular mechanism of the drug binding to the carrier protein.