Abstract
The interaction of pazufloxacin mesilate (PZFX) with catalase was studied by spectroscopic methods under simulative physiological conditions. It was observed that the PZFX quenched the intrinsic fluorescence of catalase through a static quenching procedure. Gradual addition of catalase led to a marked increase in fluorescence anisotropy ( r), it was suggested that the drug was located in a restricted environment of catalase. The negative Δ H 0 and Δ S 0 values in the case of PZFX with catalase complex implied that both hydrogen bonds and electrostatic interactions might play a significant role in PZFX binding to catalase. Circular dichorism (CD) spectra detection supported a change in the secondary structure of protein caused by the interaction of PZFX with catalase.
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