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Thromb Haemost 1981; 45(01): 055-059
DOI: 10.1055/s-0038-1650128
Original Article
Schattauer GmbH Stuttgart

Purification and Properties of an Abnormal Blood Coagulation Factor IX (Factor IXBm)/Kinetics of Its Inhibition of Factor X Activation by Factor VII and Bovine Tissue Factor

B Østerud
The Department of Medicine, University of California, San Diego, the San Diego Veterans Administration Hospital, the Department of Medicine, University of Southern California, and the Orthopaedic Hospital, Los Angeles, U.S.A.
,
C K Kasper
The Department of Medicine, University of California, San Diego, the San Diego Veterans Administration Hospital, the Department of Medicine, University of Southern California, and the Orthopaedic Hospital, Los Angeles, U.S.A.
,
K K Lavine
The Department of Medicine, University of California, San Diego, the San Diego Veterans Administration Hospital, the Department of Medicine, University of Southern California, and the Orthopaedic Hospital, Los Angeles, U.S.A.
,
C Prodanos
The Department of Medicine, University of California, San Diego, the San Diego Veterans Administration Hospital, the Department of Medicine, University of Southern California, and the Orthopaedic Hospital, Los Angeles, U.S.A.
,
S I Rapaport
The Department of Medicine, University of California, San Diego, the San Diego Veterans Administration Hospital, the Department of Medicine, University of Southern California, and the Orthopaedic Hospital, Los Angeles, U.S.A.
› Author Affiliations
Further Information

Publication History

Received 25 July 1980

Accepted 21 November 1980

Publication Date:
04 July 2018 (online)

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Summary

An abnormal blood coagulation factor IX has been isolated from the blood of a hemophilia B patient with a variant of the disease (hemophilia Bm) characterized by a normal concentration of factor IX antigen, negligible factor IX coagulant activity, and a prolonged prothrombin time with bovine tissue factor. The isolated protein (factor IXBm) had the same apparent molecular weight as normal factor IX (55,000) and the same mobility on two dimensional immunoelectrophoresis as normal factor IX. Factor IXBm underwent limited proteolysis induced by activated factor XI, in the presence of Ca2+ ions, or induced by the reaction product of tissue factor, factor VII and Ca2+ ions. A timecourse study showed that activated factor XI cleaved factor IXBm and factor IX at similar rates. However, in contrast to normal factor IX, the limited protelysis of factor IXBm did not generate procoagulant activity.

In kinetic experiments purified factor IXBm behaved like a competitive inhibitor (Ki of 0.017 μM) of the activation of factor X by bovine tissue factor and factor VII. Normal factor IX was also found to inhibit the reaction but required a four-fold higher concentration to achieve the same inhibitory effects as factor IXBm.

Keywords

Factor IXBm - Activation of factor IXBm - Inhibition kinetics
 

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