Separation of human blood plasma components exhibiting affinity to Asp-hemolysin and analyses of their binding behavior.
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概要
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The separation of plasma components capable of binding to Asp-hemolysin by affinity chromatography using a column of Sepharose 4B coupled covalently with this hemolytic toxin has been investigated.IgG, IgM and α2-macroglobulin were isolated from normal human blood plasma by this chromatography, and IgG which was eluted from the column with 1M NaCl was found to be the major component. It was also shown that Fab'fragment was able to bind to Asp-hemolysin more strongly than did the pFc'fragment and no difference was observed between the binding abilities of all IgG subclasses in vitro.Neither IgG nor its fragment influenced the hemolytic activity of Asp-hemolysin in vitro. However, the addition of α2-macroglobulin in vitro caused a marked inhibition, indicating that α2-macroglobulin is one of the plasma components inhibitory to the hemolytic activity of Asp-hemolysin.
- 日本医真菌学会の論文
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