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Thromb Haemost 1963; 09(01): 053-061
DOI: 10.1055/s-0038-1654960
Originalarbeiten — Original Articles — Travaux Originaux
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Procoagulant Material From Human Urine in Prothrombin Activation[*]

M June Caldwell
1   Department of Physiology and Pharmacology, Wayne State University, College of Medicine, Detroit, Michigan, USA, and From the Department of Medicine, University of Colorado, School of Medicine, and Belle Bonfils Memorial Blood Bank, Denver, Colorado, USA
,
Kurt N von Kaulla
1   Department of Physiology and Pharmacology, Wayne State University, College of Medicine, Detroit, Michigan, USA, and From the Department of Medicine, University of Colorado, School of Medicine, and Belle Bonfils Memorial Blood Bank, Denver, Colorado, USA
,
Edith von Kaulla
1   Department of Physiology and Pharmacology, Wayne State University, College of Medicine, Detroit, Michigan, USA, and From the Department of Medicine, University of Colorado, School of Medicine, and Belle Bonfils Memorial Blood Bank, Denver, Colorado, USA
,
Walter H Seegers
1   Department of Physiology and Pharmacology, Wayne State University, College of Medicine, Detroit, Michigan, USA, and From the Department of Medicine, University of Colorado, School of Medicine, and Belle Bonfils Memorial Blood Bank, Denver, Colorado, USA
› Author Affiliations
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Publication History

Publication Date:
21 June 2018 (online)

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Summary

The procoagulant or P fraction obtained from human urine was analyzed to determine how it functions in the activation of purified prothrombin. Prothrombin converts to thrombin in the presence of P fraction, Ac-globulin, calcium chloride and either whole platelets or platelet factor 3. The yield of thrombin can be made to depend upon the concentration of P fraction. This conversion of prothrombin to thrombin can be partially or completely inhibited by adding various concentrations of soybean trypsin inhibitor introduced into the activation mixture.

When purified prothrombin was activated with platelet factor 3 and calcium chloride, the prothrombin activity, as measured by the two-stage assay, decreased. When it was at the lowest possible level, P fraction was added. Quite quickly prothrombin activity began to reappear, and soon 100% of the original prothrombin activity was accounted for as either prothrombin-R or thrombin.

* At Wayne State University this work was supported by a research grant H-5141 from the National Heart Institute, National Institutes of Health, U. S. Public Health Service, and at the University of Colorado by grant H-5538 and The Belle Bonfils Memorial Blood Bank, Denver.


 

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