| Autor: |
Müller-Eberhard, H. J., Biro, C. E. |
| Zdroj: |
The Journal of Experimental Medicine; September 1963, Vol. 118 Issue: 3 p447-466, 20p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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