Abstract
The surface properties of the hemolytic fraction of Chironex fleckeri obtained by chromatography of tentacle extracts on Sephadex G-200 were examined for the ability of the protein to spread at the air-water interface and for its capacity to interact with and penetrate lipid and protein monolayers. The fraction was shown to have no unusual surface properties at the air-water interface which might explain its hemolytic activity. No interactions of the hemolysin with monolayers of individual components of the red cell membrane such as stromal protein, lecithin or cholesterol could be demonstrated by surface pressure and potential measurements. There appeared to be evidence of a specific complexing with a component in a mixed monolayer derived from rabbit red cell lipids. However this needs to be confirmed by further examination in monolayers prepared from individual membrane lipids.
Published Version
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