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Molecular cloning of a cDNA encoding canine factor IX
JP Evans, HH Watzke, JL Ware, DW Stafford and KA High
Department of Medicine, UNC School of Medicine, Chapel Hill 27599.
Factor IX (F.IX) is a vitamin K-dependent plasma protein, a deficiency of
which results in hemophilia B. A canine model of hemophilia B exists;
attempts to use this model for gene transfer experiments or
characterization of the hemophilic defect require elucidation of normal
canine F.IX structure. We report the isolation and characterization of the
coding region for canine F.IX cDNA. Canine F.IX possesses 86% identity at
the amino-acid level with human F.IX. The leader peptide, Gla domain, EGF
domains, and the carboxy-terminal portion of the heavy chains show
extensive sequence conservation between the canine and human. All Glu
residues undergoing gamma-carboxylation in humans are conserved in canines.
The complete coding sequence for canine F.IX has been determined, and the
derived translation product has been analyzed. A similar approach should
allow identification of the causative mutation in canine hemophilia B.
Furthermore, this clone may prove a valuable resource in gene transfer
experiments for this disease.
Volume 74,
Issue 1,
pp. 207-212,
07/01/1989
Copyright © 1989 by The American Society of Hematology
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