In vitro preparation and partial characterization of a novel complex of human fibrinogen with albumin.

Limited reduction of a mixture of purified human fibrinogen and human serum albumin leads to the formation of a stable complex. This complex is clottable with thrombin, but its electrophoretic mobility is lower than that of fibrinogen. By contrast to clots prepared from purified fibrinogen, those obtained from the complex are transparent and are completely resistant to fibrinolytic degradation induced with urokinase. In this respect the complex of fibrinogen with albumin is similar to that identified in congenitally abnormal fibrinogens.