Antigenic Character of Denatured Egg Albumin.

Abstract

The object of the present study is to determine the effect of denaturation on the immunological properties of egg albumin, and to show the relation between the albumins denatured by different methods.

The agents of denaturation used in our study are dilute acids and alkalies, alcohol and heat. Proteins denatured by these different agents have been variously called acid albumins, alkali albuminates, heat coagulated, and, alcohol coagulated proteins. Superficially these substances are similar, and previous work 1 , 2 , 3 from this laboratory has shown that they are indeed essentially the same in chemical and physical properties. This we have tried to verify by biological methods.

The acid and alkali albumins were prepared by mixing 1 per cent egg albumin solution with equal volumes of H/10 HCl and N/10 NaOH. After 2 or 3 days the denatured egg albumin was precipitated by neutralization and purified by repeated precipitation. The heat-denatured albumins were prepared by heating 100 cc. of 1 per cent egg albumin solution to which 1 cc. of N HCl or N Na₂CO₃ has been added. The acid or alkali was added to prevent flocculation. The alcohol albumin was prepared by adding 40 cc. alcohol to 50 cc. 1 per cent egg albumin to which 10 cc. of 0.3 N Na₂CO₃ have been added. This solution was allowed to stand over night before using.

In testing the antigenic character we used precipitin and anaphylactic reactions. Both reactions show that the denatured albumin, whatever be the agent of denaturation, is immunologically different from the natural albumin. The albumins denatured by different agents are closely related, though not identical.

This is a preliminary report.