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Thromb Haemost 1972; 27(01): 141-158
DOI: 10.1055/s-0038-1649349
Originalarbeiten — Original Articles — Travaux Originaux
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The Kinin System of Human Plasma

IV. The Interrelationship between the Contact Phase of Blood Coagulation and the Plasma Kinin System in Man[*]
Ayşe H. Özge-Anwar
1   The Division of Experimental Pathology, Department of Pathology, the Institute of Immunology and the Division of Hematology, Toronto General Hospital, Department of Medicine University of Toronto - Toronto, Canada
,
H. Z Movat   **
1   The Division of Experimental Pathology, Department of Pathology, the Institute of Immunology and the Division of Hematology, Toronto General Hospital, Department of Medicine University of Toronto - Toronto, Canada
,
J. G Scott
1   The Division of Experimental Pathology, Department of Pathology, the Institute of Immunology and the Division of Hematology, Toronto General Hospital, Department of Medicine University of Toronto - Toronto, Canada
› Author Affiliations
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Publication History

Publication Date:
24 July 2018 (online)

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Summary

Human plasma was adsorbed to celite. The celite eluates were chromatographed on QAE-Sephadex A-50, followed by gel filtration, isoelectric focusing and preparative polyacrylamide electrophoresis.

By anion-exchange chromatography, factor XI a, kallikrein and y-globulin were isolated from the excluded protein peak. Factor XIa (MW ∼170,000) corrected the deficiency in plasmas deficient in factors XII or XI, but had no effect on the kininsystem. Its isoelectric point was about 8.0-8.5. Kallikrein had a molecular weight of ∼ 90,000 and a pi of 7.8-8.0 The two substances could be isolated also by polyacrylamide electrophoresis.

Highly anionic fractions contained a fragment of factor XII a (prekallikrein activator), which activated prekallikrein and retained some of the clot-promoting property of the intact factor XIIa molecule. Its molecular weight was about 37,000, the pi about 4.4 and it migrated as a prealbumin by disc electrophoresis.

It is concluded that, by massive contact exposure, most of factor XII a converts to the highly anionic, low-molecular-weight prekallikrein activator. Since the prekallikrein activator is a fragment of factor XII a, we recommend that it be referred to as “XII f”.

* This study was supported by the Ontario Heart Foundation and the Medical Research Council of Canada.

* Presented in part at the 55th Annual Meeting of the American Federation Societies for Experimental Biology, Chicago April 12-17, 1971.


** This study was supported by the Ontario Heart Foundation and the Medical Research Council of Canada. Presented in part at the 55th Annual Meeting of the American Federation Societies for Experimental Biology, Chicago April 12-17, 1971.


 

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