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Modulation of TL (Thymus-Leukemia) Antigens by Fab-Fracments of TL Antibody¹

From the Department of Pathology, New York University School of Medicine, the Division of Immunology, Sloan-Kettering Institute for Cancer Research, and Sloan-Kettering Division, Cornell University Medical College, New York, New York

Abstract

Cytotoxic antibodies of H-2 and TL specificities were located in the same 7 S -globulin fraction of mouse antiserum. The anti-TL and anti-H-2 activities occurred together in antiserum fractions prepared by Sephadex G 200 gel filtration or by electrophoresis in a Geon block. The modulating activity of TL antiserum (i.e., its capacity to cause the TL + TL - phenotypic change in cells exposed to the antiserum in the absence of lytic C') also occurred in the 7 S -globulin fraction. When -globulin prepared from antiserum by Geon block electrophoresis was digested with papain, cytotoxic activity of both H-2 and TL specificities was lost, but TL modulating activity remained. Thus attachment of univalent TL antibody fragments (Fab) lacking the complement-fixing and other biologic properties of the Fc-fragment was sufficient to induce modulation. Papain digests of H-2 antibody prepared in the same way did not induce modulation of H-2 antigen or of TL antigen, indicating further that modulation of TL antigen is a specific response to TL antibody.

Footnotes

This investigation was supported by United States Public Health Service Grants CA 08627 and CA 08748 and a grant from the John A. Hartford Foundation, Inc.

² Dr. Lamm is the recipient of a Career Scientist Award of the Health Research Council of the City of New York under Contract I-474.

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