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Structure of human factor VIII

Nature volume 312, pages 337–342 (1984)Cite this article

Abstract

The deduced amino acid sequence of human factor VIII, obtained from the DNA sequence, predicts a mature polypeptide of 2,332 amino acids containing a triplicated domain structure. The polypeptide has 35% sequence homology with the copper-binding plasma protein, ceruloplasmin. Determination of the thrombin cleavage sites in plasma-derived factor VIII polypeptides allows prediction of the domains involved in the associated activation and inactivation of the protein.

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Authors and Affiliations

  1. Department of Protein Biochemistry, Genentech, Inc., 460 Point San Bruno Boulevard, South San Francisco, California, 94080, USA

    Gordon A. Vehar, Bruce Keyt, Dan Eaton, Henry Rodriguez, Rodney Keck & Richard N. Harkins

  2. Department of Molecular Biology, Genentech, Inc., 460 Point San Bruno Boulevard, South San Francisco, California, 94080, USA

    Herman Oppermann, William I. Wood, Richard M. Lawn & Daniel J. Capon

  3. Haemophilia Centre, Academic Department of Haematology, Royal Free Hospital School of Medicine, London, WC1N 1BP, UK

    Donogh P. O'Brien, Frances Rotblat & Edward G. D. Tuddenham

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  1. Gordon A. Vehar
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  2. Bruce Keyt
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Vehar, G., Keyt, B., Eaton, D. et al. Structure of human factor VIII. Nature 312, 337–342 (1984). https://doi.org/10.1038/312337a0

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