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The isolation of rapidly growing mutants from Strep. mutans JC 2 and HS 6 or Strep. salivarius SS 2 has been successfully carried out1). Previously, we reported changes in enzymatic activity correlated with cellular lyses of Strep. mutans HS 6-Ly mutant and Strep. salivarius SS 2-Ly mutant strains2). These lytic mutants were easily destroyed by H2O2 or did not lyse by addition of reducing agents. Thus, it may be speculated that these mutants do not develop protective mechanisms against oxidative damage., Glutathione peroxidase (GSH-Px) functions to detoxicate and protect cellular membranes from oxidative damage3) by coupling with the reactions of both glutathione reductase (GR) and NADP-linked glyceraldehyde 3-phosphate dehydrogenase (NADPlinked GA3PDH). To demonstrate the correlation of enzymatic activity with cellular destruction, we compared the activities of Strep mutans JC 2+, JC 2-Ly and the nonlytic mutant, JC 2-NL for both the lytic and nonlytic states. The Strep. mutans JC 2 strain was found to repair oxidative damage through enzymatic activity .

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Correlation of glutathione peroxidase-glutathione reductase-nadp-linked glyceraldehyde 3-phosphate dehydrogenase activity with cellular degradation in Strep. mutans JC2 strains.