Von Willebrand Factor: Dissociation from Antihemophilic Factor Procoagulant Activity

  title={Von Willebrand Factor: Dissociation from Antihemophilic Factor Procoagulant Activity},
  author={Harvey J. Weiss and Leon W. Hoyer},
  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.
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.
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
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
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
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.
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
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
Data from thermo‐stability and dissociation studies favour the hypothesis that factor‐VIII complex consists of two closely related but separate proteins. Expand


Factor VIII Detection by Hemagglutination Inhibition: Hemophilia A and von Willebrand's Disease
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
Molecular Forms of Antihaemophilic Globulin in Plasma, Cryoprecipitate and after Thrombin Activation
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
Defective ristocetin-induced platelet aggregation in von Willebrand's disease and its correction by factor VIII.
Patients with von Willebrand's disease are deficient in a plasma factor that is necessary for normal platelet function, and the activity of this factor appears to be associated with factor VIII but is unrelated to VIII(AHF) procoagulant activity. Expand
Immunologic studies of antihemophilic factor (AHF, factor VIII). V. Immunologic properties of AHF subunits produced by salt dissociation.
The immunologic properties of subunits obtained by sucrose density ultracentrifugation in 1 M NaCl and by agarose gel filtration in 0.24 M CaCl2 have been determined using human and rabbit anti-AHF to provide constraints which must be incorporated into models of AHF structure. Expand
Properties of the platelet retention (von Willebrand) factor and its similarity to the antihemophilic factor (AHF).
Owing to printers’ errors, the following errata appeared in the June 1973 issue of Blood (Vol. 41, No. 6). "Properties of the Platelet Retention (von Willebrand) Factor and Its Similarity to theExpand
The effect of salicylates on the hemostatic properties of platelets in man.
These studies lend further support to the hypothesis that ingestion of aspirin, in contrast to sodium salicylate, prolongs the bleeding time by inhibiting the release of platelet ADP, perhaps reflecting the findings in other cell systems which suggest that aspirin alters membrane permeability. Expand
onparaometric Staitticts NMcGraw-Hill
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Horomones anid Be/lt ior (Harper
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Supported in part by PHS grant HL 14595 and by a research girant fronm the Veterans Administration