Cleavage of Factor VIII Light Chain Is Required for Maximal Generation of Factor VIIIa Activity
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 اولProteolytic interactions of factor IXa with human factor VIII and factor VIIIa.
Factor IXa was shown to inactivate both factor VIII and factor VIIIa in a phospholipid-dependent reaction that could be blocked by an antifactor IX antibody. Factor IXa-catalyzed inactivation correlated with proteolytic cleavages within the A1 subunit of factor VIIIa and within the heavy chain (contiguous A1-A2-B domains) of factor VIII. Furthermore, a relatively slow conversion of factor VIII ...
متن کاملA2 domain of human recombinant-derived factor VIII is required for procoagulant activity but not for thrombin cleavage.
Thrombin treatment of the coagulation factor VIII results in a rapid activation of procoagulant activity with a subsequent first order decay. The structural requirements for thrombin-activated factor VIII were characterized using recombinant-derived human factor VIII and site-directed DNA-mediated mutagenesis. Thrombin-activated human recombinant-derived factor VIII was isolated in an active fo...
متن کاملMechanisms of factor Xa-catalyzed cleavage of the factor VIIIa A1 subunit resulting in cofactor inactivation.
Activation of factor VIII by factor Xa is followed by proteolytic inactivation resulting from cleavage within the A1 subunit (residues 1-372) of factor VIIIa. Factor Xa attacks two sites in A1, Arg(336), which precedes the highly acidic C-terminal region, and a recently identified site at Lys(36). By using isolated A1 subunit as substrate for proteolysis, production of the terminal fragment, A1...
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: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.15.8546