[Effect of phenylmercury derivatives on human oxyhemoglobin]

By the dynamics of human oxyhemoglobin coagulation in the presence of phenyl mercury acetate in tris-AcOH buffer, pH 7.2 the number of moles of PhHg+ stechiometrically bound with protein at different temperatures was estimated. Within the temperature range 15-30 degrees C this value is constant--32-34 mole per 1 mole of HBO2-tetramer. Within the range 30-40 degrees C it rises to approximately 40. Coagulation of oxyhemoglobin modified with PhHg+ cation is reversible in contrast to HBO2 coagulation modified with uncharged PhHgCl.