The stabilization of purified human albumin to heat

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Abstract
Purified human albumin heated in solution in 0.15 [image] NaCl at pH 6.8 develops a 2nd component. At 45[degree] and 50[degree] prolonged heating is required to modify albumin, but at 56[degree] and 60[degree] the modification is established in 1 hour. In dilute solution slight but progressive increases in viscosity were noted at 58[degree] if heating was prolonged. Solutions of 5-6.25% could be heated without gross change in viscosity, but above this protein concentration albumin gels. The action of a number of amino acids and acetyl amino acids on the heat stability of albumin was examined, but all were ineffective except acetyltryptophan, and to a lesser degree acetylphenylalanine. The stabilizing effects of different concentrations of acetyltryptophan were estimated. Solutions containing 20 mg of acetyltryptophan/g of albumin were heated for 10 hours at 60[degree] without modification of the protein. Moving-boundary electrophoresis proved more sensitive in detecting modification than electrophoresis on paper, the ultracentrifuge, or changes in viscosity.