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Immune Cryoglobulins in Rabbit Streptococcal Antiserum¹

From the Department of Preventive Medicine, Washington University School of Medicine, St. Louis, Missouri and The Rockefeller University, New York, New York

Abstract

Electrophoretic patterns of certain sera from rabbits immunized intravenously with streptococcal vaccines exhibit discrete protein bands in the -globulin region. These were identified as group-specific carbohydrate antibodies. The L-chains of these -globulins exhibited electrophoretic homogeneity. This report describes a group B immune serum which possesses unusual cryoprecipitating properties. Ninety per cent of the -globulin was cryoprotein and was distributed in two electrophoretically distinct peaks designated fast and slow. Both proteins, isolated by electrophoresis were G-globulin. The slow cryoglobulin possessed group B antibody activity. Although the fast cryoglobulin agglutinates group B cell walls the exact specificity has not been determined. Electrophoretic patterns of dissociated light chains were studied by a variety of electrophoretic techniques. By disc electrophoresis in acrylamide gel the L-chains of the slow cryoglobulin were heterogeneous and exhibited six bands. L-chains of the fast cryoglobulin were distributed in only two bands. These data suggest that immunization has resulted in the proliferation of a limited population of lymphoid cells which produced -globulin with cryoprecipitating properties.

Footnotes

This study was supported by National Institutes of Health Grants AM 08490 and HE 11112.

² Medical Scientist Fellow of the Life Insurance Medical Research Fund.

³ Special Investigator, The Arthritis Foundation.