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 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 21 Issue: 2
  • Publication Date: 2006
  • Doi Number: 10.1080/14756360500483453
  • Title of Journal : JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Page Numbers: pp.231-234

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 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.