Purification and characterization of catalase enzymes from chicken liver and sheep erythrocytes

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

ASIAN JOURNAL OF CHEMISTRY, vol.19, no.5, pp.3941-3953, 2007 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 19 Issue: 5
  • Publication Date: 2007
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.3941-3953
  • Kütahya Health Sciences University Affiliated: No


Catalase enzyme (H2O2: H2O2 oxidoreductase; E.C. was purified from chicken liver and sheep erythrocytes, using DEAE-Sephadex A50 ion exchange chromatography and some characteristics of the enzymes were investigated. The purification procedure was composed of 3 steps i.e., homogenate/hemolisate preparation, ammonium sulfate precipitation and DEAE-Sephadex A50 ion exchange chromatography. Chicken liver and sheep erythrocytes enzymes, having the specific activity of 560.46 and 1017.5 EU/mg proteins were purified with a yield of 30.06 and 22.23 %; 190.63 and 643.9-fold, respectively. In order to control the purification of enzymes were done, sodium dodecyl sulfate polyacrilamide gel electrophoresis (SDS-PAGE). SDS-PAGE showed a single band for each enzyme. Optimal pH, stable pH, optimal temperature, KM and V-max values for H2O2 were also determined for the each enzyme. In addition, molecular weight and subunit molecular weights were found by SIDS-PAGE and gel filtration chromatography respectively.