Topography of the human factor VIII-von Willebrand factor complex.

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Topography of the human factor VIII-von Willebrand factor complex.

Factor VIII circulates in noncovalent complex with von Willebrand factor (vWf). The topography of this complex was evaluated by fluorescence energy transfer using factor VIII subunits modified with N-(1-pyrenyl)maleimide (NPM; fluorescence donor) and vWf-derived fragments modified with 7-diethylamino-3-[4'-maleimidylphenyl]-4-methyl coumarin (CPM; fluorescence acceptor). Results from a previous...

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The complex multimeric composition of factor VIII/von Willebrand factor.

We have analyzed the multimeric structure of factor VIII/von Willebrand factor in plasma by sodium dodecyl sulfate electrophoresis using gels of varying porosity and a discontinuous buffer system. Factor VIII/von Willebrand factor bands were identified by reaction with 125I-labeled affinity-purified antibody and subsequent autoradiography. In 1% agarose gels, normal plasma displayed a series of...

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Lectin activity of the coagulation factor VIII/von Willebrand complex.

The human coagulation factor VIII (FVIII) is essential in the intrinsic pathway of blood coagulation and circulates mainly as a non-covalently bound complex with the von Willebrand factor (VWF). This complex (FVIII/VWF) protects FVIII from degradation and cellular uptake, although no biological role has been identified yet for this complex. The FVIII/VWF complex was purified from a healthy dono...

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Factor VIII/von Willebrand factor protein. Galactose a cryptic determinant of von Willebrand factor activity.

The normal Factor VIII/von Willebrand factor protein has the ability to agglutinate or aggregate normal platelets in the presence of ristocetin (von Willebrand factor activity). Removal of greater than 95% of the sialic acid from this protein by neuraminidase did not affect the von Willebrand factor or procoagulant activity. However, oxidation of the penultimate galactose of the asialo Factor V...

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Kinetics of factor VIII-von Willebrand factor association.

The binding of factor VIII to von Willebrand factor (vWF) is essential for the protection of factor VIII against proteolytic degradation in plasma. We have characterized the binding kinetics of human factor VIII with vWF using a centrifugation binding assay. Purified or plasma vWF was immobilized with a monoclonal antibody (MoAb RU1) covalently linked to Sepharose (Pharmacia LKB Biotechnology, ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1990

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)39310-x