The Journal of Experimental Medicine
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The Journal of Experimental Medicine, Vol 118, 447-466, Copyright © 1963, by The Rockefeller Institute

ARTICLE

ISOLATION AND DESCRIPTION OF THE FOURTH COMPONENT OF HUMAN COMPLEMENT

H. J. Müller-Eberhard M.D.1 and C. E. Biro M.D.1

1 From The Rockefeller Institute

Purification of the activity of the fourth component of human complement resulted in the isolation of a highly homogeneous serum protein. Since this protein has not been recorded previously it was called ß1E-globulin on the basis of its immunoelectrophoretic behavior. C'4 activity and ß1E-globulin were found to have highly similar, if not identical physicochemical characteristics. Moreover, ß1E-globulin was shown to exhibit the specific behavior of C'4 activity in that it is taken up only by cells which contain activated C'1. DFP-inactivated C'1 failed to catalyze uptake of the protein. Treatment with hydrazine which is known to destroy C'4 activity, led to changes in the physicochemical properties of ß1E-globulin and rendered the molecule incapable to combine with C'1-containing cells. The evidence indicates that ß1E-globulin represents the fourth component of human complement.

Submitted on May 2, 1963


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