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A New Basic Protein in Rabbit Serum Unrelated to Immunoglobulin¹

Department of Bacteriology and Immunology, University of North Carolina School of Medicine, Chapel Hill, North Carolina

Abstract

Immunoelectrophoresis of whole serum, developed with a sheep antiserum, reveals the presence in all rabbit sera of a precipitin are which is located in the slow -globulin region of the pattern. This post--globulin antigen (PGGA) is not antigenically related to IgG globulin or subunits of this protein. Absorption studies indicate that no antigenic relationship exists between PGGA and any other serum constituents. It is also distinct from rabbit lysozyme, ribonuclease and desoxyribonuclease.

This heat stable serum protein exhibits distinctive solubility properties when serum is fractionated with (NH₄)₂SO₄, Na₂SO₄, alcohol or rivanol. Elution of PGGA from Sephadex G 200 occurs after albumin, indicating a molecular weight ranging between 15,000 and 50,000. Data obtained by elution from diethylaminoethyl (DEAE)-cellulose show that PGGA may form complexes with itself or other serum proteins.

PGGA is not found in urine, colostrum or cerebrospinal fluid. Neonatal rabbit sera contain this antigen but in considerably lower concentrations than the adult.

Many IgG globulin preparations contain PGGA as a contaminant, but no antibody activity has been associated with this serum protein.

There is measurable ribonuclease activity in G-globulin preparations isolated by DEAE-Sephadex or DEAE-cellulose chromatography, as well as by alcohol precipitation.

Footnotes

This work was supported in part by Public Health Service grant AI-00949 from the National Institute of Allergy and Infectious Diseases.

² Supported by United States Public Health Service Training Grant GM-01138.