Thermochimica Acta, Vol.333, No.2, 109-114, 1999
A study on the interaction between cisplatin and urease
The present work gives the results of the interaction between cisplatin and urease. Microcalorimetry was used to measure enzymatic activity. The experimental results indicated that cisplatin could render urease inactive. Further spectral determinations showed that enzymatic 'circular dichroism' absorption peak decreased and its fluorescence was quenched by cisplatin. This proved that enzymatic secondary structure had been changed. Thermal denaturation experiments by DSC had given the same results that cisplatin resulted in the reduced denaturation enthalpy of urease, and the denaturation temperature of urease changed from 361.37 to 345.05 K under experimental conditions. It showed that cisplatin reduced enzymatic conformational stability, and the binding of cisplatin with urease was found to be a slow process.