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Amendment history:
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Free access | 10.1172/JCI105959

Studies on the prekallikrein (kallikreinogen)-kallikrein enzyme system of human plasma: I. Isolation and purification of plasma kallikreins

Robert W. Colman, Lawrence Mattler, and Sol Sherry

1Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110

Find articles by Colman, R. in: JCI | PubMed | Google Scholar

1Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110

Find articles by Mattler, L. in: JCI | PubMed | Google Scholar

1Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110

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Published January 1, 1969 - More info

Published in Volume 48, Issue 1 on January 1, 1969
J Clin Invest. 1969;48(1):11–22. https://doi.org/10.1172/JCI105959.
© 1969 The American Society for Clinical Investigation
Published January 1, 1969 - Version history
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Abstract

By measurement of its arginine esterase activity, plasma kallikrein was purified from fresh frozen ACD plasma. The steps involved alcohol fractionation, isoelectric precipitation, and carboxymethyl (CM) Sephadex and DEAE cellulose chromatography. Three enzymatically active fractions were finally isolated and termed plasma kallikreins I, II, and III; they represented purifications of 970,320- and 590-fold, respectively. All three kallikreins were active biologically; they increased vascular permeability in the guinea pig and released a kinin from human plasma, as measured in the rat uterus bioassay. Bradykinin and/or closely related kinins were identified in the kallikrein I plasma digest by radioimmunoassay.

Kallikreins I, II, and III had similar ratios of hydrolytic activity on a variety of arginine and lysine esters and were immunochemically related. However, differences were present on physicochemical characterization: kallikrein I had S20,[unk] of 5.7, a mol wt of 99,800, and migrated as a slow gamma globulin; kallikrein II migrated as a fast gamma globulin with a mol wt of 163,000, but the evidence suggested that it was closely related, if not interconvertible, with kallikrein I. Kallikrein III, on the other hand, migrated as an alpha globulin and reacted quite differently with inhibitors.

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Referenced in 7 patents
1 readers on Mendeley
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