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Research Article Free access | 10.1172/JCI107313

Inhibition by CāINH of Hageman Factor Fragment Activation of Coagulation, Fibrinolysis, and Kinin Generation

Alan D. Schreiber, Allen P. Kaplan, and K. Frank Austen

Department of Medicine, Harvard Medical School, Boston, Massachusetts 02120

Department of Medicine Robert B. Brigham Hospital, Boston, Massachusetts 02120

Find articles by Schreiber, A. in: PubMed | Google Scholar

Department of Medicine, Harvard Medical School, Boston, Massachusetts 02120

Department of Medicine Robert B. Brigham Hospital, Boston, Massachusetts 02120

Find articles by Kaplan, A. in: PubMed | Google Scholar

Department of Medicine, Harvard Medical School, Boston, Massachusetts 02120

Department of Medicine Robert B. Brigham Hospital, Boston, Massachusetts 02120

Find articles by Austen, K. in: PubMed | Google Scholar

Published June 1, 1973 - More info

Published in Volume 52, Issue 6 on June 1, 1973
J Clin Invest. 1973;52(6):1402–1409. https://doi.org/10.1172/JCI107313.
© 1973 The American Society for Clinical Investigation
Published June 1, 1973 - Version history
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Abstract

Highly purified inhibitor of the first component of complement (CāINH) was shown to inhibit the capacity of active Hageman factor fragments to initiate kinin generation, fibrinolysis, and coagulation. The inhibition of prealbumin Hageman factor fragments observed was dependent upon the time of interaction of the fragments with CāINH and not to an effect upon kallikrein or plasmin generated. The inhibition of the coagulant activity of the intermediate sized Hageman factor fragment by CāINH was not due to an effect on PTA or other clotting factors. The inhibition by CāINH of both the prealbumin and intermediate sized Hageman factor fragments occurred in a dose response fashion. The CāINH did not appear to be consumed when the activity of the Hageman factor fragments was blocked, although the fragments themselves could no longer be recovered functionally or as a protein on alkaline disc gel electrophoretic analysis. These results suggest that the CāINH may have an enzymatic effect on the fragments or that an additional site on CāINH is involved in Cā inactivation.

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