Von Willebrand Factor: Dissociation from Antihemophilic Factor Procoagulant Activity

@article{Weiss1973VonWF,
  title={Von Willebrand Factor: Dissociation from Antihemophilic Factor Procoagulant Activity},
  author={Harvey J. Weiss and Leon W. Hoyer},
  journal={Science},
  year={1973},
  volume={182},
  pages={1149 - 1151}
}
Factor VIII corrects both the clotting defect in hemophilia A and an abnormality of platelet aggregation in von Willebrand's disease. These two activities of factor VIII (antihemophilic factor and von Willebrand factor) are both detected in the void volume when human plasma or cryoprecipitate is chromatographed on Bio-Gel 5M under conditions of isotonic salt concentration. In contrast, antihemophilic factor procoagulant activity is detected with proteins of lower molecular weight when the… Expand
Dispersity of human factor VIII--Von Willebrand factor.
TLDR
Changes in the polymer distribution of factor VIII-Von Willebrand factor can be an alternative explanation for results of dissociation experiments and for abnormalities in various diseases as demonstrated by cross-immunoelectrophoresis. Expand
Studies of the human factor VIII/von Willebrand's factor protein. II. Identification and characterization of the von Willebrand protein.
TLDR
The purified factor VIII-related protein, previously characterized from normal cryoprecipitate, possesses both procoagulant activity and vWf activity and should be designated the f VIII/vWf protein. Expand
Separation of human factor VIII activity from the von willebrand's antigen and ristocetin platelet aggregating activity
Abstract Factor VIII coagulant activity was separated by ion-exchange chromatography from the von Willebrand's antigen (Factor VIII-like antigen). The von Willebrand's antigen was also separated fromExpand
Evidence that functional subunits of antihemophilic factor (Factor VIII) are linked by noncovalent bonds.
Partially purified human antihemophilic factor (AHF, factor VIII), when treated with high concentrations of salt, has been shown to dissociate into two components: one, of relatively low molecularExpand
Molecular pathology and immunology of factor VIII (hemophilia A and factor VIII inhibitors).
  • L. Hoyer
  • Biology, Medicine
  • Human pathology
  • 1987
TLDR
Although the antibodies cause a serious problem for affected individuals, they have been very useful in characterizing normal factor VIII and nonfunctional factor VIII-like protein that is found in the plasmas of 10 per cent of patients with mild hemophilia. Expand
The factor VIII complex: structure and function.
  • L. Hoyer
  • Chemistry, Medicine
  • Progress in clinical and biological research
  • 1981
TLDR
The information now available permits a preliminary understanding of the molecular defects in the factor VIII deficiency disease. Expand
Recent Advances in Haemophilia and Von Willebrand's Disease 1
TLDR
The advances in the biochemistry and immunology of AHF have stimulated new considerations of the relationship between that factor and vWf and their molecular biology but the picture is far from clear. Expand
Interaction of factor VIII antigen in hemophilic plasmas with human antibodies to factor VIII.
TLDR
Data suggest that there are greater antigenic similarities between normal and hemophilic Factor VIII than previously thought. Expand
Factor VIII Procoagulant and Antigen Content of Antihemophilic Factor (AHF) Concentrates
TLDR
Antihemophilic factor concentrates from six manufacturers were studied for factor VIII procoagulant and antigen content, indicating a significant loss of activity during the fractionation process. Expand
Willebrand Factor and Ristocetin II. RELATIONSHIP BETWEEN WILLEBRAND FACTOR, WILLEBRAND ANTIGEN AND FACTOR‐VIII ACTIVITY
TLDR
Data from thermo‐stability and dissociation studies favour the hypothesis that factor‐VIII complex consists of two closely related but separate proteins. Expand
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Factor VIII activity was detected immunologically in both the serums and plasmas of 14 normal individuals and 14 patients with hemophilia A, indicating that the test may serve as a specific assay for differentiation between von Willebrand's disease and hemophili A. Expand
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Sedimentation characteristics of factor VIII were investigated by ultracentrifugation in 10–40% w/v sucrose gradient in pH 7.2 and immunological analysis of this fraction failed to reveal the presence of any fibrinogen, suggesting that fast‐sedimenting factor VIII is a non‐covalently bound polymer. Expand
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TLDR
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Supported in part by PHS grant HL 14595 and by a research girant fronm the Veterans Administration