Abstract
HUMAN factor VIII contains at least two biological activities, antihaemophilic factor (AHF) and von Willebrand factor (VWF). When highly purified, factor VIII is estimated to have a molecular weight of over 1.12 × 106, as determined by gel chromatography or sedimentation equilibrium centrifugation1–4. Some investigators2–4 consider factor VIII a single glycoprotein with a number of covalently linked subunits. Since factor VIII can be dissociated in certain conditions, others5–7 consider it to be a two-molecule complex consisting of a multi-subunit high molecular weight protein (> 106) with VWF activity that acts as a carrier molecule for a lower molecular weight (2.4 × 105) subunit with AHF activity. A third model suggests that both AHF and VWF are high molecular weight, separate proteins consisting of disulphide linked subunits8,9.
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NEWMAN, J., HARRIS, R. & JOHNSON, A. Molecular weights of antihaemophilic factor and von Willebrand factor proteins in human plasma. Nature 263, 612–613 (1976). https://doi.org/10.1038/263612a0
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DOI: https://doi.org/10.1038/263612a0
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