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In a previous publication we reported a method for the preparation of a heat stable human plasma protein solution (1). The method was a modification of that of Cohn, Strong, Hughes, Mulford, Ashworth, Melin, and Taylor (2) and used ethanol-water mixtures at low temperatures for the separation of the heat labile crude fibrinogen fraction (Fraction I) and gamma globulin fraction (Fraction II + III) from normal human plasma. The supernatant fluid following the removal of the crude gammaglobulin fraction was dried from the frozen state and reconstituted to plasma volume with distilled water. Heating of this material for 10 hours at 600 C. changed the optical density at 550 mF and the electrophoretic distribution very little. Electrophoretically, the heated material was 80 per cent albumin, 16 per cent alpha globulin and 4 per cent beta globulin. Heating of the solution for 10 hours at 600 C. caused the formation of a small amount of a very fast moving component in the ultracentrifuge. The remainder representing approximately 90 per cent of the starting protein concentration was homogeneous and had an uncorrected sedimentation constant of approximately 4.0 x 1018. . The present communication concerns the heat stability of human plasma protein solutions remaining following the precipitation of the Fraction II + III proteins from normal human plasma by different ethanol concentrations and temperatures.

HEAT STABILITY OF PROTEIN SOLUTIONS OBTAINED FROM HUMAN PLASMA BY DIFFERENT ETHANOL CONCENTRATIONS AND TEMPERATURES 1