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The Influence of Non-Specific Protein on the Heat Inactivation of Antibody to Pneumococcal Polysaccharide

I. Effect of Various Proteins on the Heat Stability of Antibody¹

From the Biochemical Research Foundation of the Franklin Institute, Newark, Delaware

Abstract

1. Water-insoluble globulin from a sample of Type I antipneumococcal horse serum was found to be more heat resistant than the parent serum as regards retention of specific precipitability.

2. Restoration of the serum components removed in purification, or addition of whole serum to the water insoluble-globulin solution, resulted in mixtures which were inactivated under conditions which did not inactivate the antibody alone.

3. Heating the water-insoluble globulin and the other serum components separately before mixing did not interfere with specific precipitation.

4. The ability to assist in heat inactivation of antipneumococcal antibody appeared to be a property associated primarily with the non-antibody serum globulin.

5. Casein, also, possessed this property to a marked degree.

6. Gelatin, albumin, myogen, pectin, gum arabic, and heterologous polysaccharide had no effect upon the heat-inactivation of antibody.

Footnotes

¹ The material in this and in the following article was presented at the Boston meeting of the American Association of Immunologists, April 2, 1942.