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.

This content is only available as a PDF.