Immunochemical characterization of fibrinogen, fibrin I, and fibrin II in human thrombi and atherosclerotic lesions
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چکیده
منابع مشابه
Immunochemical characterization of fibrinogen, fibrin I, and fibrin II in human thrombi and atherosclerotic lesions.
Arterial thrombi and atherosclerotic lesions were analyzed immunochemically and examined histologically. The extent of in vivo proteolytic cleavage of the amino-terminal end of fibrinogen by thrombin and plasmin was determined and quantitated by specific radioimmunoassays. The samples were treated with cyanogen bromide (CNBr), and the total amount of fibrinogen and fibrin-derived protein was de...
متن کاملImmunochemical Characterization of Fibrinogen , Fibrin I , and Fibrin II in Human
Arterial thrombi and atherosclerotic lesions were analyzed immunochemically and examined histologically. The extent of in vivo proteolytic cleavage of the amino-terminal end of fibrinogen by thrombin and plasmin was determined and quantitated by specific radioimmunoassays. The samples were treated with cyanogen bromide (CNBr). and the total amount of fibrinogen and fibrin-derived protein was de...
متن کاملCharacterization of fragment E from fibrinogen and cross-linked fibrin.
Fragment E, a terminal plasmin digestion product of fibrinogen or fibrin, contains portions of the alpha, beta, and gamma chains linked by disulfide bonds. In this study, Fragment E from fibrinogen and fully cross-linked fibrin were purified by gel filtration of the soluble fraction from heated plasmin digests of either fibrinogen or fibrin or by step-wise chromatography of terminal plasmin dig...
متن کاملFibrinogen-fibrin degradation products.
The identification of the molecular structure of fibrinogen has given a better understanding of many clinical conditions associated with abnormalities of fibrinogen. Proteolysis of fibrinogen or fibrin by its natural lytic enzyme, plasmin, leads to the formation of degradation products which are of great importance in the laboratory diagnosis of many pathological conditions. The biochemical and...
متن کاملSubunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin.
The three unique polypeptide chains of human fibrinogen differ significantly in molecular weight. Cross-linkage of fibrin by fibrin-stabilizing factor results in the rapid formation of cross-links between gamma-chains and a slower formation of cross-links between alpha-chains. beta-Chains are not involved directly in the cross-linking of fibrin. Reduced, cross-linked fibrin contains uncross-lin...
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ژورنال
عنوان ژورنال: Blood
سال: 1987
ISSN: 0006-4971,1528-0020
DOI: 10.1182/blood.v69.4.1038.bloodjournal6941038