The Interface between the EGF2 Domain and the Protease Domain in Blood Coagulation Factor IX Contributes to Factor VIII Binding and Factor X Activation

Biochemistry ◽  
2006 ◽  
Vol 45 (35) ◽  
pp. 10777-10785 ◽  
Author(s):  
Caroline Fribourg ◽  
Alexander B. Meijer ◽  
Koen Mertens
Keyword(s):  
Factor Viii ◽  
Blood Coagulation ◽  
Coagulation Factor ◽  
Factor Ix ◽  
Factor X ◽  
Protease Domain ◽  
Coagulation Factor Ix ◽  
Factor X Activation

Prediction of the secondary structures of bovine blood coagulation factor IX, factor X, and prothrombin

1988 ◽  
Vol 7 (5) ◽  
pp. 613-632
Author(s):  
John M. Beals ◽  
Joseph Weber ◽  
Paul Derwent ◽  
Kenneth L. Grant ◽  
Francis J. Castellino
Keyword(s):  
Blood Coagulation ◽  
Coagulation Factor ◽  
Secondary Structures ◽  
Factor Ix ◽  
Factor X ◽  
Bovine Blood ◽  
Coagulation Factor Ix

scholarly journals Cleavage at Arginine 145 in Human Blood Coagulation Factor IX Converts the Zymogen into a Factor VIII Binding Enzyme

1995 ◽  
Vol 270 (25) ◽  
pp. 14884-14890 ◽  
Author(s):  
Peter J. Lenting ◽  
Hans ter Maat ◽  
Patrick P. F. M. Clijsters ◽  
Marie-José S. H. Donath ◽  
Jan A. van Mourik ◽  
...  
Keyword(s):  
Factor Viii ◽  
Blood Coagulation ◽  
Human Blood ◽  
Coagulation Factor ◽  
Factor Ix ◽  
Coagulation Factor Ix ◽  
Human Blood Coagulation

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

1981 ◽  
Vol 45 (01) ◽  
pp. 055-059 ◽  
Author(s):  
B Østerud ◽  
C K Kasper ◽  
K K Lavine ◽  
C Prodanos ◽  
S I Rapaport
Keyword(s):  
Tissue Factor ◽  
Blood Coagulation ◽  
Limited Proteolysis ◽  
Coagulation Factor ◽  
Factor Ix ◽  
Factor Vii ◽  
Factor X ◽  
Factor Xi ◽  
Coagulation Factor Ix ◽  
Bovine Tissue

SummaryAn 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.

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