Proceedings: A new fibrinolytic enzyme: the prolixase. Physicochemical and biological properties.
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Biomedical subjects
Publications and source records attributed to C Soria.
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Studies were performed to analyse the inhibitory effect of a myeloma globulin (IgG) on fibrin formation. This inhibitory activity was very intense and caused a severe bleeding disorder which proved fatal. The isolated myeloma globulin inhibited all three stages of fibrin formation: the proteolytic action of thrombin on fibrinogen, the aggregation of fibrin monomers and the stabilization of fibrin by cross-linkages in the gamma and alpha chains. Purified factor XIII, even in excess, previously activated by the addition of thrombin and calcium, did not correct this defect in cross linking. Our results suggest that this myeloma globulin induced a blockage of some receptors near the cross linking sites.
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A case of an acquired circulating anticoagulant occurring in a patient suffering from chronic lymphocytic leukaemia with haemolytic anaemia and autoimmune disorders has been reported. The anticoagulant was found to belong to the IgM class. Coagulation studies show that this anticoagulant inhibits the reaction between human prothrombinase andfactor II.
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