pH-dependent denaturation of thrombin-activated porcine factor VIII.
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چکیده
منابع مشابه
pH-dependent denaturation of thrombin-activated porcine factor VIII.
Thrombin-activated porcine factor VIII (fVIIIaIIa) is a stable, active, 160-kDa heterotrimer at concentrations exceeding 2 x 10(-7) M in 0.7 M NaCl, 0.01 M histidine Cl, 5 mM CaCl2, pH 6.0, at 4 degrees C or 20 degrees C. Two of the subunits, fVIIIA1 and fVIIIA2, are derived from the heavy chain of the plasma-derived, heterodimeric fVIII precursor. The third subunit, fVIIIA3-C1-C2, is derived f...
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The activation of porcine factor X by an enzymatic complex consisting of activated factor IX (factor IXa). thrombinactivated factor VIll:C (factor Vlll:Ca). phospholipid vesides. and calcium was studied in the presence of an irreversible inhibitor of factor Xa. 5-dimethylamino-naphthalene-1 -sulfonyl-glutamyl-glycyl-arginyl-chloromethyl ketone (DEGR-CK). The formation of factor Xa was measured ...
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We studied the activation of factor X by the intrinsic pathway of blood coagulation using a new assay of factor X activation. When factor X tritiated in its sialic acid residues is activated, activation can be measured by the release of tritiated activation peptide, and the initial rate of activation can be determined under varying conditions. In the presence of phospholipid and calcium ions, f...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)40071-9