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Volume 271, Number 45, Issue of November 8, 1996 pp. 28601-28606
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Factor X_{St. Louis II}
IDENTIFICATION OF A GLYCINE SUBSTITUTION AT RESIDUE 7 AND CHARACTERIZATION OF THE RECOMBINANT PROTEIN

(Received for publication, July 23, 1996)

From the Departments of Pathology and Medicine, Division of Laboratory Medicine, Washington University School of Medicine, St. Louis, Missouri 63110

A molecular defect in factor X (fX) results from a point mutation that causes glycine substitution for -carboxylated glutamic acid at position 7. The variant (fX_{St. Louis II}) and wild type (fX_WT) proteins were produced in a mammalian expression system and characterized. fX_{St. Louis II} has <1% and ~3% of normal clotting activity in modified prothrombin time and partial thromboplastin time assays, respectively. The rate of activation of fX_{St. Louis II} by factor VIIa and tissue factor is undetectable under conditions that result in complete activation of fX_WT; activation by factors VIIIa and IXa is ~30% of normal activation. The X-activating protein from Russell's viper venom activates fX_{St. Louis II} completely but at a reduced rate. Thrombin generation on phoshopolipid vesicles or activated platelets is ~30% or ~5%, respectively. Membrane-dependent autolysis is markedly reduced for fX_{St. Louis II}. In reactions that are not surface-dependent, fX_{St. Louis II} is nearly identical to that of fX_WT. The rate of inhibition by antithrombin is indistiguishable, as is the rate of thrombin formation in the absence of phospholipid, with or without factor Va.

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