[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.

[Microcolorimetric study of the association of trypsin with a pancreatic inhibitor].

Enthalpy of the association of trypsin with pancreatic inhibitor from bovine pancreas at 25 degrees C as a function of pH and ionic strength is estimated. The dependence of the enthalpy on pH is of an extremal character with a minimum at pH 7.6 (delta H degrees =-10.