Characterization of the functional defect in factor IX Alabama. Evidence for a conformational change due to high affinity calcium binding in the first epidermal growth factor domain.-Reference-Cited by-同舟云学术

Characterization of the functional defect in factor IX Alabama. Evidence for a conformational change due to high affinity calcium binding in the first epidermal growth factor domain.

Published:1990-06 Issue:18 Volume:265 Page:10250-10254
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

McCord D M,Monroe D M,Smith K J,Roberts H R

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference44 articles.

1. Isolation and characterization of a cDNA coding for human factor IX.

2. Activation of human factor IX (Christmas factor).

3. Activation of factor IX by the reaction product of tissue factor and factor VII: additional pathway for initiating blood coagulation.

4. Redetermination of the rate-limiting step in the activation of factor IX by factor XIa and by factor VIIa/tissue factor. Explanation for different electrophoretic radioactivity profiles obtained on activation of 3H- and 125I-labeled factor IX

5. Blood Coagulation

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