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

Abstract

Catalase enzyme (H2O2: oxidoreductase; E.C. 1.11.1.6) was purified from human skin homogenate using ammonium sulfate precipitation and DEAE-Sephadex A50 ion exchange chromatography at 4°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. © 2006 Taylor & Francis.