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Primary structure of vitamin K-dependent human protein Z
H Sejima1, T Hayashi, Y Deyashiki
1Division of Enzyme Cytology, Institute for Enzyme Research, University of Tokushima, Japan.
Biochemical and Biophysical Research Communications
|September 14, 1990
Abstract:
The primary structure of a vitamin K-dependent human protein Z was determined by a combination of analyses of 41 amino acid residues of the NH2-terminal region and 1265 nucleotide base pairs of a cDNA encoding the residual COOH-terminal part of the protein and the 3' noncoding region. Human protein Z has 360 amino acid residues which is less than that of bovine protein Z containing 396 residues. Human protein Z was composed of an NH2-terminal domain rich in gamma-carboxyglutamic acids, two epidermal growth factor-like domains and a COOH-terminal serine protease-like domain as was bovine protein Z.