The interaction of dextran with serum albumin, gamma globulin, and fibrinogen.

The interaction between dextran and serum albumin, gamma globulin, and fibrinogen can be studied by an electrophoretic method, which depends on obtaining electrophoretic patterns, first of each protein, then of dextran, and finally of mixtures of each protein with dextran. The areas under the electrophoretic spikes for each protein, for dextran, and for the mixtures are measured. At pH's between 9.6 and 6.6, there is a transference of albumin to dextran when the two components are mixed, the amount of albumin lost being nearly equal to the gain in the new component, albumin plus dextran. This new species has a specific refractive index of about 0.00205 and seems to be composed of about one albumin molecule for every four dextran molecules. The method is unsuitable for studying interaction between dextran and gamma globulin because these substances are almost immobile and do not separate into two spikes. The method shows that a mixture of dextran and fibrinogen gives only one slowly moving spike (pH 6.6 to 8.6), the area under which is the sum of the areas under the dextran and the fibrinogen spikes taken separately. Either there is no interaction, or the new species has virtually the same refractive index increment as fibrinogen and dextran taken separately (0.0014 to 0.0015).