Effects of pH, ionic strength and temperature on the ovalbuminanti-ovalbumin precipitin reaction.

  • 1 September 1973
    • journal article
    • Vol. 25  (3) , 377-83
Abstract
A detailed study of the effects of pH, ionic strength, and temperature on the ovalbumin—anti-ovalbumin precipitin reaction was made. The optimal pH range for the precipitation was 6.6–8.3. The profile of the precipitin reaction was found to be identical to that of a typical enzyme catalysed reaction, and suggested the involvement of two types of ionizable groups on either ovalbumin or anti-ovalbumin molecule. Maximum precipitation was observed near physiological ionic strength, i.e. 0.15 I. The course as well as the extent of the precipitin reaction was favoured by an increase in temperature from 0° to 45°. Further increase in temperature from 45° to 60° caused appreciable decrease in the precipitation. Results on the effect of temperature on the precipitin reaction were interpreted in terms of the involvement of hydrophobic interaction between non-polar amino acid side chains of ovalbumin and anti-ovalbumin molecules, in the reaction.