CLINICAL STUDIES ON ANTITHROMBIN
نویسندگان
چکیده
منابع مشابه
Structural studies on the carbohydrate portion of human antithrombin III.
Human antithrombin III has been shown to contain four identical N-glycosidically linked carbohydrate chain per molecule. These carbohydrate chains have been investigated by sugar and methylation analysis before and after removal of N-acetylneuraminic acid residues. The chains have been further investigated by Smith degradation, trifluoroacetolytic degradation, and degradation after chromium tri...
متن کاملAntithrombin: anti-inflammatory properties and clinical applications.
Many humoral and cellular components participate in bidirectional communication between the coagulation and inflammation pathways. Natural anticoagulant proteins, including antithrombin (AT), tissue factor pathway inhibitor, and protein C, suppress proinflammatory mediators. Conversely, inflammation blunts anticoagulant activity and, when uncontrolled, promotes systemic inflammation-induced coa...
متن کاملClinical studies on progressive retinal atrophy in 31 dogs
During a 2-year period, 31 cases of a hereditary retinal degeneration in dogs bred in India were found mainly suspected for progressive retinal atrophy (PRA) with typical history of initial nyctalopia followed by hemeralopia. Out of 31 PRA suspected dogs, 8 dogs (26%) were from the age group of 1-5 years, 15 (48%) 6-10 years and the rest (26%) 11-15 years. The most predominant breed was Spitz (...
متن کاملCurrent perspective on antithrombin drugs.
Thrombin is a multifunctional serine protease, which is involved in blood coagulation and thrombosis, inflammation and wound repair in tissue injury. Its role in the amelioration of inflammatory tissue injury has been investigated. Protease-activated cell surface receptors (PARs) when activated by thrombin result in the production of proinflammatory mediators. In the kidney, these PARs are expr...
متن کاملUpdate on antithrombin I (fibrin).
Antithrombin I (fibrin) is an important inhibitor of thrombin generation that functions by sequestering thrombin in the forming fibrin clot, and also by reducing the catalytic activity of fibrinbound thrombin. Thrombin binding to fibrin takes place at two classes of non-substrate sites: 1) in the fibrin E domain (two per molecule) through interaction with thrombin exosite 1; 2) at a single site...
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ژورنال
عنوان ژورنال: The KITAKANTO Medical Journal
سال: 1959
ISSN: 0023-1908,1883-6135
DOI: 10.2974/kmj1951.9.1226