In vitro effects of some drugs on catalase purified from human skin

Altıkat S., Çoban T. A., Çiftci M., Özdemir H.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, vol.21, no.2, pp.231-234, 2006 (SCI-Expanded) identifier identifier identifier


Catalase enzyme (H2O2: oxidoreductase; E.C. was purified from human skin homogenate using ammonium sulfate precipitation and DEAE-Sephadex A50 ion exchange chromatography at 4 degrees C and some characteristics of the enzyme were investigated. The human skin enzyme, having a specific activity of 1354.5 EU/mg proteins was purified with a yield of 43.13% and 1110-fold. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed a single band for the enzyme. Inhibition by piroxicam, ketoprofen, diclofenac sodium, sulfamethoxazole and nidazole occurred with I-50 values of 0.414 1.29, 1.8, 3.83, and 8.64 mM, respectively.