Studies on the Mechanism of Action of Oxygen-labile Haemolysins

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Abstract
The sensitivities of the binding step and the lytic step of hemolysis by pneumolysin to the action of various inhibitors and to variations in the assay conditions were studied. Binding was inhibited by HgCl2 and N-ethylmaleimide. Lysis by previously fixed lysin was insensitive to HgCl2 and only slightly sensitive to N-ethylmaleimide. Binding of pneumolysin was independent of ionic strength. Binding of pneumolysin and streptolysin O decrease above pH 8.0 and 8.4, respectively. Binding may require a non-ionized unsubstituted sulfhydryl group. Incubation of [rabbit] erythrocytes with NaF caused inhibition of pneumolysis, indicating that some metabolic function of the cell may be involved in lysis. The action of streptolysin O was not affected by NaF.