Quantification of plasma factor XIIa-Cl(-)-inhibitor and kallikrein-Cl(- )-inhibitor complexes in sepsis
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چکیده
منابع مشابه
Complexes Between Cl - Inhibitor , Kallikrein , High Molecular Weight Kininogen
When normal human plasma was adsorbed at 4 C with monosEecific antibody globulins to human Cl -INH inhibitor (anti-Cl -INH). Cl -INH was removed from the plasma in proportion to the amount of antibody globulins used. Clotting activity attributable to Fletcher factor (prekallikreinh high molecular weight kininogen (HMW-K). and irregularly. plasma thromboplastin antecedent (PTA. factor Xl) were a...
متن کاملComplexes Between Cl - Inhibitor , Kallikrein , High Molecular Weight Kininogen , Plasma Thromboplastin
When normal human plasma was adsorbed at 4 C with monosEecific antibody globulins to human Cl -INH inhibitor (anti-Cl -INH). Cl -INH was removed from the plasma in proportion to the amount of antibody globulins used. Clotting activity attributable to Fletcher factor (prekallikreinh high molecular weight kininogen (HMW-K). and irregularly. plasma thromboplastin antecedent (PTA. factor Xl) were a...
متن کاملInactivation of Factor XIa in Human Plasma Assessed by Measuring Factor XIa-Protease Inhibitor Complexes: Major Role for Cl-Inhibitor
From experiments with purified proteins, it has been concluded that factor Xla (FXla) is inhibited in plasma mainly by a,-antitrypsin (alAT), followed by antithrombin 111 (ATIll), Cl-inhibitor (Cllnh), and a2-antiplasmin (a2AP). However, the validity of this concept has never been studied n plasma. We established the relative contribution of different inhibitors to the inactivation of FXla in h...
متن کاملNewand Rapid Functional Assay for Cl Inhibitor in Human Plasma
c i’ inhibitor (Ci-INH) and a2-macroglobulin (a2M) account for over 90% of the inactivation of purified plasma kallikrein by normal human plasma. The rate of kallikrein inactivation is also dependent on the presence of high molecular weight kininogen (HMWK). which forms a reversible complex with kallikrein protecting the active site of the enzyme against inhibitors. By selectively mactivating a...
متن کاملInactivation of purified human alpha 2-antiplasmin and purified human C1 inhibitor by synthetic fibrinolytic agents.
3-Hydroxypropyl flufenamide (Flu-HPA) is one of a series of flufenamic acid derivatives that enhances blood clot lysis in vitro. Studies of possible mechanisms of action of Flu-HPA were undertaken. The profibrinolytic activity of Flu-HPA in clot lysis assays was found to be dependent on plasminogen. The influence of Flu-HPA on the ability of purified alpha 2-antiplasmin to inhibit purified plas...
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ژورنال
عنوان ژورنال: Blood
سال: 1988
ISSN: 0006-4971,1528-0020
DOI: 10.1182/blood.v72.6.1841.1841