Abstract
The interaction of jack bean urease with dodecyl trimethylammonium bromide (DTAB), tetradecyl trimethylammonium bromide (TTAB), and hexadecyl trimethylammonium bromide (HTAB) was studied by microcalorimetry at T= 300 K and equilibrium dialysis at temperatures of 300 K and 310 K in alkaline solution at PH = 10.0. The enthalpy of binding was calculated from binding data with were obtained from equilibrium dialysis in terms of the Wyman binding potential theory related to the van't Hoff relation. The enthalpy of urease unfolding was determined by subtraction of the microcalorimetric enthalpy (binding and unfolding enthalpies) and the enthalpy of binding. The enthalpy of urease unfolding, in the presence of DTAB, TTAB, and HTAB, was 7200 kJ·mol −1.
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