Purification and characterization of catalase from goat (Capra capra) lung

Mol Cell Biochem. 1993 Sep 22;126(2):125-33. doi: 10.1007/BF00925690.


Catalase plays a major role in the protection of tissues from toxic effects of H2O2 and partially reduced oxygen species. In the present study catalase was extracted and purified 330-fold from goat lung by acetone fractionation and successive chromatographies on DEAE-cellulose, Sephadex G-200, Blue Sepharose CL-6B and Ultrogel AcA-34. The purified enzyme was almost homogeneous as judged by polyacrylamide gel electrophoresis and FPLC. The molecular weight and Stokes' radius of the purified enzyme were 339 kDa and 127 +/- 2 A. The enzyme had 11 sulfhydryl groups and 15 tryptophan groups per mol of the enzyme. A broad pH optimum in the range 5.2 to 7.8 was obtained. Sulfhydryl group binding agents, thiol reagents and N-Bromosuccinimide inhibited the enzyme activity. The kinetic data show no cooperativity between the substrate binding sites. Tryptophan, indole acetic acid, cysteine, formaldehyde and sodium azide inhibited the enzyme non-competitively with Ki values of 1.5, 1.6, 6.7, 0.55 and 0.0017 mM, respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / pharmacology
  • Animals
  • Bromosuccinimide / pharmacology
  • Catalase / chemistry*
  • Catalase / drug effects
  • Catalase / isolation & purification
  • Catalase / metabolism
  • Goats / metabolism*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Lung / enzymology*
  • Molecular Weight
  • Sulfhydryl Compounds / analysis
  • Sulfhydryl Compounds / pharmacology
  • Sulfhydryl Reagents / pharmacology
  • Tryptophan / analysis


  • Amino Acids
  • Sulfhydryl Compounds
  • Sulfhydryl Reagents
  • Tryptophan
  • Catalase
  • Bromosuccinimide