Isolation and characterization of vitamin K-dependent region of bovine blood clotting factor X.
A 39-residue peptide from the tryptic digestion of bovine blood clotting factor X has been isolated by specific adsorption on barium citrate. The amino- and carboxyl-terminal sequences of the peptide were determined and compared to the vitamin K-dependent Ca2+-binding region from bovine prothrombin. The factor X peptide was found to contain gamma-carboxyglutamic acid residues, and the results of independent analysis are consistent with all 14 glutamic acid residues as gamma-carboxyglutamic acid. The similarity of the factor X peptide to the prothrombin peptide supports the hypothesis that the vitamin K-dependent blood clotting proteins are descended from a common ancestral gene.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002118:Calcium; D002417:Cattle; D002852:Chromatography, Ion Exchange; D005170:Factor X / Q000302:isolation & purification; D010446:Peptide Fragments; D011485:Protein Binding; D011955:Receptors, Drug; D014357:Trypsin; D014812:Vitamin K
D000596:Amino Acids; D010446:Peptide Fragments; D011955:Receptors, Drug; D014812:Vitamin K; D005170:Factor X; D014357:Trypsin; D002118:Calcium