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The Inactivation of Human C1 by Benzamidine and Pyridinium Sulfonylfluorides¹

Center for Blood Research, 800 Huntington Avenue, Boston, Massachusetts 02115, and the Department of Chemistry, University of California at Santa Barbara, Santa Barbara, California 93106

Abstract

Affinity chromatographically purified C was demonstrated to be inhibitable by a variety of benzamidine and pyridinium fluorosulfonyl-substituted compounds. Four of the compounds tested afforded greater than 50% inhibition at concentrations between 10^-6 and 10^-5 M. The data indicated that inhibition was greatest with those compounds which contained a substituted benzamidine and sulfonyl-fluoride group. The site of action was the esterase activity associated with the C1.

Footnotes

¹ This work was supported by grants from the National Institutes of Health, Grant 7-R01-AM17351-01, and Damon Runyon Memorial Fund, DRG 1167. Preliminary results of this study were reported in April 1973 at the annual meeting of the American Association of Immunologists in Atlantic City, New Jersey.

² To whom reprint requests should be addressed. Recipient Research Career Development Award 1-K04-AM-F-0340-ALY.

³ Address: Bioorganic Chemistry Department, Stanford Research Institute, Menlo Park, California 94025.