The Journal of Experimental Medicine
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The Journal of Experimental Medicine, Vol 138, 438-451, Copyright © 1973 by The Rockefeller University Press

ARTICLE

THE MEMBRANE ATTACK MECHANISM OF COMPLEMENT : VERIFICATION OF A STABLE C5-9 COMPLEX IN FREE SOLUTION



William P. Kolb 1 and Hans J. Müller-Eberhard 1

1 From the Department of Experimental Pathology, Scripps Clinic and Research Foundation, La Jolla, California 92037

The membrane attack mechanism of complement, C5 to C9, has previously been postulated to associate on the target cell surface to a stable decamolecular complex with a calculated mol wt of 995,000.

A soluble and stable complex consisting of C5, C6, C7, C8, and C9 has now been demonstrated to arise as a consequence of complement activation by the classical or alternate pathway. It has a sedimentation coefficient of 22.5S and a mol wt of 1 million daltons, and it migrates on electrophoresis at pH 8.6 as an alpha-globulin.

The stable and soluble C5b-9 complex cannot bind to erythrocytes and has no demonstrable cytolytic activity. However, due to partially unsaturated binding sites for C9, it can bind additional C9 and thus function as an inhibitor of lysis of EAC1-8 by C9.

These results support the concept according to which the membrane-bound attack system of complement represents a stable, decamolecular assembly of C5b-9. Unlike its analogue in free solution, the membrane-bound complex is cytolytically active.

 Submitted on April 15, 1973


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