Studies on the mechanism of action of oxygen-labile haemolysins.
The sensitivities of the binding step and the lytic step of haemolysis 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 decreased above pH 8-0 and 8-4 respectively. These results suggest that binding requires a non-ionized unsubstituted sulphydryl group. Incubation of erythrocytes with NaF caused inhibition of pneumolysin, indicating that some metabolic function of the cell may be involved in lysis. The action of streptolysin O was not affected by NaF.
D001665:Binding Sites / Q000187:drug effects; D006460:Hemolysin Proteins / Q000378:metabolism*; D006461:Hemolysis / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D009994:Osmolar Concentration; D012969:Sodium Fluoride / Q000494:pharmacology; D013439:Sulfhydryl Reagents / Q000494:pharmacology
D006460:Hemolysin Proteins; D013439:Sulfhydryl Reagents; D012969:Sodium Fluoride