Abstract
The influence of EACA on C1 in whole human serum and on C1 and C1̄ as isolated molecules was assessed hemolytically. There was selective inhibition of C1 without effect on the levels of C4, C2, C3, and C9 in whole human serum that was reversed by dialysis. EACA was found to inhibit the intrinsic activation of C1 without inhibiting the already active molecule. This was confirmed by the capacity of trypsin to uncover C1 activity in cellular intermediates formed by C1 treated with EACA that did not evolve in the absence of this extrinsic activating mechanism. Inasmuch as the trypsin-dependent recovery of C1 was incomplete, an effect on binding cannot be excluded.
Footnotes
-
↵2 Dr. Soter is a Postgraduate Fellow of the Dermatology Foundation.
-
↵3 Dr. Gigli is the recipient of Research Career-Development Award AM-46409 from the National Institutes of Health.
-
↵1 This work was supported in part by Grants RR-05489, AI-07722, and AM-05577 from the National Institutes of Health.
- Received September 23, 1974.
- Copyright © 1975 by The American Association of Immunologists, Inc.
Pay Per Article - You may access this article (from the computer you are currently using) for 1 day for US$37.50
Regain Access - You can regain access to a recent Pay per Article purchase if your access period has not yet expired.
Log in using your username and password
In this issue
