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

Abstract:

: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.

journal_name

Mol Cell Biochem

authors

Chatterjee U,Sanwal GG

doi

10.1007/BF00925690

subject

Has Abstract

pub_date

1993-09-22 00:00:00

pages

125-33

issue

2

eissn

0300-8177

issn

1573-4919

journal_volume

126

pub_type

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