Ca2+ Binding to the First Epidermal Growth Factor-like Domain of Human Blood Coagulation Factor IX Promotes Enzyme Activity and Factor VIII Light Chain Binding
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چکیده
منابع مشابه
Functional and Molecular Characterization of C91S Mutation in the Second Epidermal Growth Factor-like Domain of Factor VII
Background: Coagulation Factor VII is a vitamin K-dependent serine protease which has a pivotal role in the initiation of the coagulation cascade. The congenital Factor VII deficiency is a recessive hemorrhagic disorder that occurs due to mutations of F7 gene. In the present study C91S (p.C91S) substitution was detected in a patient with FVII deficiency. This mutation has not b...
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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 اولSome human inhibitor antibodies interfere with factor VIII binding to factor IX.
Factor VIII (fVIII) functions as a cofactor of factor IXa in the intrinsic pathway of blood coagulation. Its absence or abnormality causes the bleeding disorder hemophilia A. About 23% of hemophiliacs who receive therapeutic fVIII infusions develop antibodies that inhibit its activity. We previously showed by inhibitor neutralization assays that the fVIII A2 and C2 domain polypeptides contain c...
متن کاملRegions 301-303 and 333-339 in the catalytic domain of blood coagulation factor IX are factor VIII-interactive sites involved in stimulation of enzyme activity.
The contribution of the Factor IX catalytic domain to Factor VIIIa binding has been evaluated by functional analysis of Factor IX variants with substitutions in alpha-helix region 333-339 and region 301-303. These regions were found to play a prominent role in Factor VIIIa-dependent stimulation of Factor X activation, but do not contribute to the high-affinity interaction with Factor VIIIa ligh...
متن کاملDevelopment of aptameric affinity ligands specific to human plasma coagulation factor VIII using SEC-SELEX
Protein specific aptamers are highly applicable affinity ligands in different fields of research and clinical applications. They have been developed against various targets, in particular, bio-macromolecules such as proteins. Among human proteins, the coagulation factors are the most attractive targets for aptamer selection and their specific aptamers had valuable characteristics in therapeutic...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.41.25332