Abstract
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 β1E-globulin on the basis of its immunoelectrophoretic behavior. C'4 activity and β1E-globulin were found to have highly similar, if not identical physicochemical characteristics. Moreover, β1E-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 β1E-globulin and rendered the molecule incapable to combine with C'1-containing cells. The evidence indicates that β1E-globulin represents the fourth component of human complement.
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Selected References
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