Affiliation:
1. Division of Bacterial Products, Bureau of Biologics, Food and Drug Administration, Bethesda, Maryland 20014
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.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
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