No abstract

Tetanolysin, partially purified, caused the lysis of human and rabbit platelets, as determined by a decrease in the optical density of platelet suspensions and the release of serotonin, enzymes, and protein. This lytic activity was neutralized by antitoxin. In addition, a suspension of the lysosome-containing large granule fraction of rabbit liver released hydrolytic enzymes when exposed to tetanolysin. Thus, tetanolysin can be added to the list of bacterial toxins that are lytic for a variety of cellular or subcellular membranes. These findings provide additional data that suggest that tetanolysin may contribute to the pathogenesis of some of the unusual manifestations observed in clinical tetanus.