A unique factor XIII inhibitor to a fibrin-binding site on factor XIIIA
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چکیده
منابع مشابه
A unique factor XIII inhibitor to a fibrin-binding site on factor XIIIA.
An 81-year-old woman, who presented with sudden episodes of spontaneous bleeding, was found to have a specific inhibitor of factor XIII. Her fibrin clots had approximately 70% gamma-gamma and no alpha polymer formation, under conditions where normal fibrin was fully cross-linked; the patient's clots were soluble in urea or monochloroacetic acid. Factor XIII activity in her plasma was 24%, measu...
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An 81-year-old woman, who presented with sudden episodes of spontaneous bleeding, was found to have a specific inhibitor of factor XIII. Her fibrin clots had 70% y y and no a polymer formation, under conditions where normal fibrin was fully cross-linked; the patient’s clots were soluble in urea or monochloroacetic acid. Factor Xll l activity in her plasma was 24%. measured by the dansylcadaveri...
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Fibrin polymers (des A,B fibrinogen) reduced the concentration of a-thrombin required for 50% activation of plasma factor XIII (a2b2 tetramer) by approximately 1 00-fold. In the presence of fibrin, the amount of ‘y-thrombin required for activation was not affected. Catalytically inactive i-Pr2Pand D-Phe-PrO-Arg-CH2-a-thrOmbin were found to inhibit over 95% of the activation by a-thrombin in the...
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http://bloodjournal.hematologylibrary.org/content/91/1/149.full.html Updated information and services can be found at: (2497 articles) Hemostasis, Thrombosis, and Vascular Biology Articles on similar topics can be found in the following Blood collections http://bloodjournal.hematologylibrary.org/site/misc/rights.xhtml#repub_requests Information about reproducing this article in parts or in i...
متن کاملFactor XIIIa formation promoted by complexing of alpha-thrombin, fibrin, and plasma factor XIII.
Fibrin polymers (des A,B fibrinogen) reduced the concentration of alpha-thrombin required for 50% activation of plasma factor XIII (a2b2 tetramer) by approximately 100-fold. In the presence of fibrin, the amount of gamma-thrombin required for activation was not affected. Catalytically inactive i-Pr2P- and D-Phe-Pro-Arg-CH2-alpha-thrombin were found to inhibit over 95% of the activation by alpha...
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ژورنال
عنوان ژورنال: Blood
سال: 1992
ISSN: 0006-4971,1528-0020
DOI: 10.1182/blood.v79.1.65.65