Abstract
Factor IX is a plasma glycoprotein with m.w. 57,000. It is a single chain precurser to a serine protease which participates in the middle phase of blood coagulation. It is activated by factor XIa (activated factor XI) as well as by a complex of factor VII-tissue factor to a two chain form serine protease, factor IXa. Factor IX is one of the half a dozen blood proteins which require vitamin K for their normal biosynthesis. These proteins include factor VII, factor IX, factor X, prothrombin, protein C, protein S and protein Z. The first four proteins are blood coagulation factors. Protein C functions as an efficient regulator of blood coagulation by inactivating factors Villa and Va in the presence of protein S. Protein S also has a possible regulatory role in the complement system by binding to C4b binding2 protein. The function for protein Z is not known at the present time. The first about ten glutamic acid residues which are located within the amino-terminal about 40 amino acid sequence of these proteins are converted to gamma carboxylglutamic acid residues (gla residues) in a reaction catalyzed by a membrane-bound carboxylase(s) in the presence of vitamin K as a cofactor3. These gla residues in the proteins serve as the sites to bind calcium ions which are required for the optimal activities for these proteins.
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References
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Kurachi, K., Chen, SH. (1987). Human Genes for Factor IX and other Vitamin K Dependent Blood Proteins. In: Wessler, S., Becker, C.G., Nemerson, Y. (eds) The New Dimensions of Warfarin Prophylaxis. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-5985-3_6
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DOI: https://doi.org/10.1007/978-1-4757-5985-3_6
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