The Binding of Calcium Ions to Bovine Factor X by Rate Dialysis

التفاصيل البيبلوغرافية
العنوان: The Binding of Calcium Ions to Bovine Factor X by Rate Dialysis
المؤلفون: Menard M. Gertler, Robert H. Yue
المصدر: Thrombosis and Haemostasis. 40:350-357
بيانات النشر: Georg Thieme Verlag KG, 1978.
سنة النشر: 1978
مصطلحات موضوعية: Protease, Factor X, medicine.medical_treatment, Substrate (chemistry), chemistry.chemical_element, Hematology, Calcium, Dissociation constant, chemistry.chemical_compound, Crystallography, chemistry, Zymogen, Mole, medicine, Binding site
الوصف: SummaryThe binding of Ca+2 to bovine factor X (molecular weight of 74,000) (Yue und Gertler 1977) was studied by the technique of rate dialysis and with the use of 45Ca+2. The binding data are consistent with a model of sequential mechanism. One mole of Ca+2 binds to the glycoprotein with a dissociation constant of 5.2 × 10-5 M and an additional 39 ± 4 moles of Ca+2 bind to this zymogen with a dissociation constant of 3.7 × 10-3M. The binding of the high affinity Ca+2 causes a functionally significant change in the zymogen, and (calcium) (factor X) complex is the real substrate in the activation process by the protease in Russell’s viper venom.
تدمد: 2567-689X
0340-6245
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::c4467c67c4f8e75576bd78f78d89138d
https://doi.org/10.1055/s-0038-1648668
رقم الأكسشن: edsair.doi...........c4467c67c4f8e75576bd78f78d89138d
قاعدة البيانات: OpenAIRE