Crossed immunoelectrophoretic pre-peak of canine factor VIII-related antigen

Bass, Arthur I.; Benson, Roger E.; Dodds, W J

doi:10.1016/0049-3848(80)90237-6

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Factor Viii/von Willebrand Factor: Antihemophilic Factor (Ah1

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1981

1997

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Cited by 10 publications

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“…Since then, five more reports have been published. One deals with canine [264] and the others with human variants of the vWF [261][262][263]. Analysis of the defect was ob tained by crossed IEP [261][262][263] and by gel electro phoresis [263].…”

Section: Factor Viii/von Willebrand Factor: Antihemophilic Factor (Ahmentioning

confidence: 99%

Antibody Technics and Blood Coagulation

Hassouna¹,

Penner

1981

Semin Thromb Hemost

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Section: Factor Viii/von Willebrand Factor: Antihemophilic Factor (Ahmentioning

confidence: 99%

Antibody Technics and Blood Coagulation

Hassouna¹,

Penner

1981

Semin Thromb Hemost

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Conformational changes in von Willebrand's factor protein: Effects on the binding of factor VIII‐coagulant

1986

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The effects of conformational changes in purified canine von Willebrand's factor (VWF) were investigated to explore the relationship between its factor VIII-related antigen (VIII:AG) and ristocetin cofactor (RCoF) properties and the factor VIII-coagulant (VIII:C) binding site(s). Binding of VIII:C from canine von Willebrand's disease (VWD) plasma by VWF was used to measure the combining reaction of these proteins. The VWF was denatured to varying degrees by exposure to temperature and pH extremes, low ionic strength, and 6 M urea. Various treatments resulted in three types of change: elimination of RCoF, VIIIR:Ag, and VIII:C binding, removal of RCoF activity alone; or elimination of RCoF and retarded elution of VIII:Ag and VIII:C. As long as VIIIR:Ag reactivity was maintained, binding of VIII:C could be demonstrated; but in the absence of VIIIR:Ag, neither RCoF activity nor VIII:C binding remained. These results suggest that VIII:C binding and RCoF sites are separate on VWF and that interaction between VIII:C and VWF is possible even after significant structural changes occur in VWF. Furthermore, RCoF is more vulnerable to denaturation than the antigenic site. The spectrum of conformational changes that affect the properties of VWF may parallel the various recognized subtypes of VWD.

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