Thromb Haemost 1996; 75(03): 481-487
DOI: 10.1055/s-0038-1650301
Original Article
Schattauer GmbH Stuttgart

Characterization of a cDNA Encoding Murine Coagulation Factor VII

Authors

  • Esohe Idusogie

    1   The Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA
  • Elliot Rosen

    1   The Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA
    2   The Center for Transgene Technology and Gene Therapy, Flanders Interuniversity Institute for Biotechnology, KU Leuven, Belgium
  • Jie-Ping Geng

    1   The Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA
  • Peter Carmeliet

    2   The Center for Transgene Technology and Gene Therapy, Flanders Interuniversity Institute for Biotechnology, KU Leuven, Belgium
  • Desirá Collen

    2   The Center for Transgene Technology and Gene Therapy, Flanders Interuniversity Institute for Biotechnology, KU Leuven, Belgium
  • Francis J Castellino

    1   The Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA
Further Information

Publication History

Received 31 August 1995

Accepted after revision 13 December 1995

Publication Date:
27 July 2018 (online)

Preview

Summary

The cDNA encoding murine coagulation factor VII (mfVII) was isolated and reconstructed from a Λ Zap cDNA library generated from murine liver mRNA. The cDNA contains 1903 nucleotides spanning 15 bases upstream of the 5’-translation initiation codon, an open reading frame of 1338 nucleotides, 550 nucleotides downstream of the first stop codon and a 3’ poly(A) tail. The translation product is composed of a 41-amino acid signal/propeptide region followed by a 405-residue mature protein. The latter is highly homologous to that of human, rabbit, bovine, Rhesus monkey, and canine fVII. All protein domains of hfVII are strictly conserved in mfVII.