Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Effects of Cysteine on the Inactivation of Bovine Liver Catalase

  • R. Yousefi ;
  • A. A. Saboury ;
  • M. Ghadermarzi ;
  • A. A. Moosavi-Movahedi
  • Published : 20000600
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Abstract

Bovine liver catalase was exposed to cysteine, as a natural inactivator metabolize, causing autoxidation-generating $H_2O_2$ continuously. The catalase species concentrations and activity measurement were done by spectrophotometry in phosphate buffer 10mM, pH 6.5, and 27 $^{\circ}C$. The activity of catalase decreased continuously due to the conversion of active ferricatalase species, E-Fe (III), to an inactive enzyme species, E-Fe (IV). This conversion is related to the slow production of $H_2O_2generated$ by autoxidation of cysteine. The free SH-group of cysteine has an essential role in production of $H_2O_2$ and hence inactivation of catalase. NADPH can protect catalase against inactivation due to the conversion of inactive form of E-Fe (IV) to ferricatalase species, E-Fe (III).

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