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Science 11 November 1988:
Vol. 242. no. 4880, pp. 939 - 941
DOI: 10.1126/science.3187533
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Articles

Science, Vol 242, Issue 4880, 939-941
Copyright © 1988 by American Association for the Advancement of Science

articles

Ovothiol replaces glutathione peroxidase as a hydrogen peroxide scavenger in sea urchin eggs

E Turner, LJ Hager, and BM Shapiro

Department of Biochemistry, University of Washington, Seattle 98195.

Despite its potential toxicity, H2O2 is used as an extracellular oxidant by Stronglylocentrotus purpuratus eggs to cross-link their fertilization envelopes. These eggs contain 5 mM 1-methyl-N alpha,N alpha-dimethyl-4-mercaptohistidine (ovothiol C), which reacts with H2O2. In consuming H2O2 and being reduced by glutathione, ovothiol acts as a glutathione peroxidase and replaces the function of the enzyme in eggs. The ovothiol system is more effective than egg catalase in destroying H2O2 at concentrations produced during fertilization and constitutes a principal mechanism for preventing oxidative damage at fertilization.


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