A new vitamin K-dependent protein. Purification from bovine plasma and preliminary characterization.
Four proteins active in blood coagulation have long been known to require vitamin K for their proper biosynthesis: factors II, VII, IX, and X. This paper describes the purification of a hitherto unrecognized vitamin K-dependent glycoprotein from bovine plasma. The biosynthesis of this protein is interfered with by the vitamin K antagonist Dicoumarol. The molecular weight of the protein is approximately 56,000 and, like factor X, it has two polypeptide chains. The light chain binds Ca2+. Its NH2-terminal amino acid sequence is homologous to the NH2-terminal sequences of the other vitamin K-dependent proteins and it contains vitamin K-dependent gamma-carboxyglutamic acid residues. The biological function of this protein is unknown.
D000117:Acetylglucosamine / Q000032:analysis; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001779:Blood Coagulation Factors / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D007122:Immunoelectrophoresis; D014812:Vitamin K / Q000494:pharmacology*
D000596:Amino Acids; D001779:Blood Coagulation Factors; D014812:Vitamin K; D000117:Acetylglucosamine