Dysproteinemia Induced in Vitro by Plasmin Digestion of Fibrinogen

Abstract

1. Electrophoretic investigation of split products of plasmin digestion of pure fibrinogen and of fibrinogen in a plasma medium was performed. It was shown that split products possessed electrophoretic mobilities of alpha, beta and gamma globulins. 2. It could be shown that by digestion of I¹³¹-labeled fibrinogen, radioactivity in the range of alpha, beta and gamma globulins is released. 3. Simultaneously with the formation of high molecular intermediates, low molecular, TCA-soluble substances are released. 4. Radioactivity balance calculation of the relative amounts of the newly formed fractions has been performed. 5. A possible influence of plasmin-induced fibrinogen proteolysis on the electrophoretic pattern of plasma proteins in dysproteinemia has been suggested. 6. The electrophoretic pattern of plasma proteins, obtained in the above experiments is similar to those seen in patients with dysproteinemia.