Von Willebrand factor protects the Ca2+-dependent structure of the factor VIII light chain
نویسندگان
چکیده
منابع مشابه
von Willebrand factor is a cofactor for thrombin-catalyzed cleavage of the factor VIII light chain.
The proteolytic activation of highly purified, heterodimeric porcine factor VIII and factor VIII-von Willebrand factor complex by thrombin was compared at I 0.17, pH 7.0, 22 degrees C. During the activation of factor VIII, heavy-chain cleavage is necessary to activate the procoagulant function, whereas light-chain cleavage is required to dissociate factor VIII from von Willebrand factor. The ki...
متن کاملfactor influencing the adoption of internet banking
دوره مشترک کارشناسی ارشد بازاریابی و تجارت الکترونیک دانشگاه تربیت مدرس_ دانشگاه تکنولوژی lule? چکیده پایان نامه عوامل موثر بر پذیرش اینترنت بانک توسط مشتریان پیشرفت فناوری اطلاعات و ارتباطات و به طور خاص رشد اینترنت جهت تراکنش های معاملات بازرگانی، تاثیر بسیار عمیقی در صنعت بانکداری داشته است.این در حالی ست که نفوذ بانکداری اینترنتی در کشورهای در حال توسعه بسیار کندتر از نفوذ آن ...
15 صفحه اولThe 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...
متن کاملTopography 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...
متن کاملFactor 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...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: British Journal of Haematology
سال: 2009
ISSN: 0007-1048,1365-2141
DOI: 10.1111/j.1365-2141.2009.07792.x