Abstract
Summary
Preparations of Cytochrome c from horse heart or beef heart were potent inhibitors of growth of Micrococcus lysodeikticus. Preparations of oxidized Cytochrome c from either beef heart or horse heart increased stability of lysozyme activity to heat under certain conditions. Cytochrome c reduced by Na2S2O4 does not appear to stabilize lysozyme activity to heat. Protection of lysozyme activity by oxidized Cytochrome c is afforded from 28°C to 60°C in solutions buffered at pH 5.0 to 90 minutes. Excellent protection is afforded also to aqueous, unbuffered solutions at 100°C for incubation of 10 minutes. The optimal molecular ratio for exertion of beneficial effects upon lysozyme appears to be about 10 molecules of Cytochrome c to 1 of lysozyme. Under certain conditions Cytochrome c preparations appear to exert a slight stimulation of initial velocity of lysis by lysozyme.
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