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The anticlotting properties of the fungal protease EL 25-79 have been assayed using freshly collected human and bovine blood and sodium-citrate-treated samples. 0.1% EL 25-79 was sufficient to prevent clotting. At this concentration, the protease provokes only a limited proteolysis of major plasma proteins, and at the same time does not digest the hemoglobin contained in the erythrocyte, because it is protected by the cell membrane. The kinetic studies on the enzyme action were performed using both fibrinogen and albumin. The data show that the ratio between the initial velocity of hydrolysis of human fibrinogen and human albumin at enzyme concentrations close to zero is 85. The SDS PAGE analyses of the protein patterns of the corresponding samples for the kinetic study confirmed these data.

A multi-component MSA with non-additive radii (NAR-MSA) is applied to the study of monodisperse polyelectrolyte suspensions, described within the primitive model. The NAR-MSA is analytically solvable, and in practice permits an easy implementation of a rescaled MSA (RMSA). The polyion-polyion structure factor that one obtains compares favorably with the available results of more demanding mixed integral equations. Also, the treatment of all ions on an equivalent footing allows an easy evaluation of the thermodynamic properties of the solution, and hence investigation of liquid-liquid phase transitions.