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.
Article|
September 01 1963
ISOLATION AND DESCRIPTION OF THE FOURTH COMPONENT OF HUMAN COMPLEMENT
H. J. Müller-Eberhard,
H. J. Müller-Eberhard
From The Rockefeller Institute
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C. E. Biro
C. E. Biro
From The Rockefeller Institute
Search for other works by this author on:
H. J. Müller-Eberhard
From The Rockefeller Institute
C. E. Biro
From The Rockefeller Institute
Received:
May 02 1963
Online ISSN: 1540-9538
Print ISSN: 0022-1007
Copyright © 1963, by The Rockefeller Institute
1963
J Exp Med (1963) 118 (3): 447–466.
Article history
Received:
May 02 1963
Citation
H. J. Müller-Eberhard, C. E. Biro; ISOLATION AND DESCRIPTION OF THE FOURTH COMPONENT OF HUMAN COMPLEMENT . J Exp Med 1 September 1963; 118 (3): 447–466. doi: https://doi.org/10.1084/jem.118.3.447
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