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Thromb Haemost 1979; 42(03): 855-863
DOI: 10.1055/s-0038-1666934
Original Article
Schattauer GmbH Stuttgart

Purification and Properties of an Antiactivator Fraction from Bovine Serum

L B Nanninga
The Department of Physiology and Biophysics, University of Texas Medical Branch, Galveston, Texas 77550, U.S.A.
,
M M Guest
The Department of Physiology and Biophysics, University of Texas Medical Branch, Galveston, Texas 77550, U.S.A.
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Publikationsverlauf

Received 06. Juli 1978

Accepted 18. Dezember 1978

Publikationsdatum:
23. August 2018 (online)

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Summary

A method is described for the purification of antiactivator from bovine euglobulin-free serum by means of gelfiltration and ion exchange chromatography. The purified antiactivator has no antifibrinolytic activity. It has a molecular weight of about 115,000 and it appears to be a gamma globulin. The dissociation constant of its complex with urokinase is 1.6 X 10-9 M and the maximum urokinase binding is close to 2000 CTA units per mg. Its concentration in bovine serum is 0.37%. Flufenamate displaces urokinase from the antiactivator at very low concentrations, about 10-4 M. Cysteine restores its activity if lost by standing. Also an antifibrinolysin fraction is obtained free of antiactivator activity.

 

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