PMID: 3763597Nov 1, 1986Paper

The mechanism of peroxidase-mediated cytotoxicity. I. Comparison of horseradish peroxidase and lactoperoxidase

Proceedings of the Society for Experimental Biology and Medicine
S J McFaulJohannes Everse

Abstract

The kinetics of the cytolytic activity expressed by lactoperoxidase and horseradish peroxidase toward erythrocytes in the presence of H2O2 and iodide have been investigated at physiological pH. The action of both enzymes was found to be very similar with respect to their kinetic mechanisms. Both enzymes showed saturation kinetics at higher enzyme concentrations under conditions where substrate concentrations were not limiting. Optimal concentrations of H2O2 and iodide were found to be 40 and 25 microM, respectively, for both enzymes. Higher concentrations of H2O2 inhibited the cytolytic activity. The pH dependence of the cytolytic reaction is also very similar for both enzymes, showing maximal activity at about pH 6.3. Moreover, the cytolytic activities of both enzymes were inhibited by tyrosine, tryptophan, cysteine, and to a lesser extent by histidine. We conclude from these data that the mechanisms of horseradish peroxidase and lactoperoxidase in promoting the lysis of erythrocytes are closely related if not identical.

Citations

Jan 1, 1997·Free Radical Biology & Medicine·J Everse, N Hsia
Sep 24, 2004·Free Radical Biology & Medicine·Johannes Everse, Penelope W Coates
Mar 1, 1987·Analytical Biochemistry·H Lin, J Everse
Dec 1, 1990·Archives of Biochemistry and Biophysics·A I VoznesenskyA I Archakov
May 31, 2011·Biochimica Et Biophysica Acta·Johannes EversePenelope W Coates
Jan 1, 1995·Artificial Cells, Blood Substitutes, and Immobilization Biotechnology·J R Hess
Sep 1, 1996·Artificial Cells, Blood Substitutes, and Immobilization Biotechnology·N Hsia, J Everse
May 1, 1997·Antimicrobial Agents and Chemotherapy·M Lis, H K Kuramitsu

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