Format

Send to:

Choose Destination
See comment in PubMed Commons below
Biochem Biophys Res Commun. 1990 Sep 14;171(2):661-8.

Primary structure of vitamin K-dependent human protein Z.

Author information

  • 1Division of Enzyme Cytology, Institute for Enzyme Research, University of Tokushima, Japan.

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.

PMID:
2403355
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk