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Characterization of Complexes Which Contain Diphtheria Toxin and Human Nonprecipitating Antitoxin¹

From the Central Blood Bank of Pittsburgh and the Departments of Pathology and Biophysics, University of Pittsburgh, Pittsburgh, Pennsylvania

Abstract

Complexes which contained nonprecipitating diphtheria antitoxin and I¹³¹ toxin were analyzed for sedimentation behavior in the ultracentrifuge. When high-speed centrifugation was employed using a separation cell, it was found that sedimentation of the complex was fastest at six-fold antibody excess and slowest at antibody equivalence as judged by relative percentages of I¹³¹ in upper and lower portions of the cell. When studied electrophoretically using the technique of zone electrophoresis, it was found that complexes at equivalence or in antibody excess remained close to the point of application, but migrated toward the anode when in antigen excess. Approximate sedimentation constants for the different toxin-antitoxin combinations are presented. The use of labelled antigens and physicochemical methods in the purification of nonprecipitating antibody are discussed.

Footnotes

The work described in this paper has been supported by grants-in-aid from the American Heart Association and the United States Public Health Service.