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

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Abstract
Different ethanol concentrations and temperatures were used to remove the crude gamma globulin containing fraction (Fraction II/III) from human plasma in preparation of heat stable human plasma protein solutions. When ethanol concentrations were less than 25% and temperatures were higher than -5[degree]C, the plasmaprotein solutions following 10 hours heating at 60 C showed a new component in the electrophoresis patterns, an increased amount of a very fast moving component in the ultracentrifuge and a change in optical density. When the ethanol concentration used was 25% and the temperature was -5 C, the resulting plasma protein solution following 10 hours heating at 60 C showed none of the new component in the electrophoresis patterns, much less of the very fast moving component in the ultracentrifuge and much less change in optical density. The stabilizers, acetyl-DL-tryptophanate and caprylate, had little stabilizing effect on the solutions heated at 60[degree]C for 10 hours.