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JBC, Vol. 251, Issue 2, 355-363, Jan, 1976
J. Stenflo
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.
A new vitamin K-dependent protein. Purification from bovine plasma and preliminary characterization
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