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Homocytotropic Antibody Response in the Rat Infected with the Nematode, Nippostrongylus Brasiliensis

III. Characteristics of the Antibody¹

From the Department of Medicine, Harvard Medical School, the Arthritis Unit of the Department of Medicine, Massachusetts General Hospital, and the Department of Tropical Public Health, Harvard School of Public Health, Boston, Massachusetts

Abstract

Homocytotropic antibodies produced by the rat in response to infection with N. brasiliensis were found to be heat-labile and susceptible to inactivation by 2-mercaptoethanol. On electrophoresis in agar at pH 8.6, H.A. migrated faster than the bulk of G-, A- and M-globulins. The molecular size of H.A. appeared to be somewhat greater than that of 7 S, but smaller than 19 S globulins. On diethylaminoethyl cellulose chromatography, H.A. was eluted with the peak concentration of A-globulins. H.A. activity was removed from rat antiserum by absorption with rabbit antiserum to rat immunoglobulins.

Although available evidence suggests that H.A. constitutes a unique rat immunoglobulin class analogous to human E, final assignment should be delayed until the characteristics of the heavy polypeptide chains of rat H.A. have been determined.

Footnotes

This publication is No. 447 of the Robert W. Lovett Memorial Group for the Study of Crippling Diseases, Harvard Medical School, at the Massachusetts General Hospital, Boston, Massachusetts.

This work was supported in part by Grant A100177 from the National Institute of Allergy and Infectious Diseases, United States Public Health Service, the American Cancer Society, Massachusetts Division and the Medical Research Council, London.

² Senior Investigator, Arthritis Foundation.

³ Research Fellow, Harvard School of Public Health; on leave from National Institute of Research, Mill Hill, London.