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Research Article Free access | 10.1172/JCI106962

Inhibitors of Kallikrein in Human Plasma

David J. McConnell

1Department of Medicine, Columbia University College of Physicians and Surgeons, New York 10032

Find articles by McConnell, D. in: PubMed | Google Scholar

Published July 1, 1972 - More info

Published in Volume 51, Issue 7 on July 1, 1972
J Clin Invest. 1972;51(7):1611–1623. https://doi.org/10.1172/JCI106962.
© 1972 The American Society for Clinical Investigation
Published July 1, 1972 - Version history
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Abstract

Human plasma was fractionated by ammonium sulfate precipitation, DEAE-cellulose chromatography, and Sephadex G-200 gel filtration to determine which method would give the greatest number of clearly separable kallikrein inhibitory peaks. With G-200 gel filtration three peaks could be separated which were demonstrated to contain α2-macroglobulin, C1̄ inactivator, and α1-antitrypsin. No other kallikrein inhibitors could be identified. The fractions containing C1̄ inactivator and α2-macroglobulin appeared to be more effective against kallikrein than that containing α1-antitrypsin. A patient with hereditary angioneurotic edema was shown to have an abnormal C1̄ inactivator protein capable of interfering with kallikrein's biologic, but not its esterolytic activity. Heat-treated human plasma, a commonly used source of kininogen for experiments with kallikrein, was shown to have kallikrein inhibitory activity.

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