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The Journal of Immunology, Vol 124, Issue 6 2824-2827, Copyright © 1980 by American Association of Immunologists
ARTICLES |
MD Boyle and SH Ohanian
The failure of functionally purified C5gp to reconstitute the hemolytic complement (C) activity of C5-deficient human serum was studied. The lack of hemolytic activity of C5gp in this system could not be correlated with the failure of EAC1-3hu to bind and activate C5gp, but was related to the failure of EAC1-3hu5gp6hu to efficiently bind C7hu in a form that would lead to lysis when HuC8 and HuC9 were added. This failure was not observed with EAC1-3gp5gp6hu or EAC1-3hu5hu6hu, which could be lysed with any combination of human or guinea pig C7 through C9. The implications of these findings on the control of the lytic C attack mechanism by the initial components in the C cascade are discussed.
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