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The Journal of Immunology, 1968, 101: 1159-1167.
Copyright © 1968 by The American Association of Immunologists, Inc.
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Antigenic Heterogeneity of Reduced and Alkylated Subunits of Human Monoclonal Macroglobulins1

Carlos J. Dominguez2, Vincent Caggiano, Shaul Kochwa and Louis R. Wasserman

Department of Hematology, Mount Sinai Hospital, and the Department of Medicine, Mount Sinai School of Medicine, New York, New York

Abstract

Twenty-two isolated human monoclonal macroglobulins were studied by several immuno- and physicochemical methods. The size of the subunits dissociated by thiols and alkylated by monoiodoacetamide depended on the concentration of the reducing agent and the time of reduction. Immunochemical analysis performed with an antiserum prepared in rabbits against one of the proteins (reagent 17a) indicated that the subunits of individual macroglobulins are antigenically heterogeneous. Two antigenic determinants detected by this antiserum can be found on different subunits of native macroglobulins following mild reduction and alkylation. These antigenic determinants vary in their relative concentration and are destroyed by high concentrations of thiol. Alkylation of the reduced protein leaves an additional, common, and separable antigenic determinant, which persists after heavy reduction and alkylation and is independent of the light chain type of the native macroglobulin.

Footnotes

This study was supported in part by United States Public Health Service Grants AM-04434, CA-04457, CA-05126, PH-43-67-1359 from the National Cancer Institute, the National Institute of Arthritis and Metabolic Diseases and the National Heart Institute, and by the Albert A. List, Frederic Machlin and Anna Ruth Lowenberg Research Funds.

2 Senior Clinical Trainee United States Public Health Service Cancer Control Program Award CST 413 B67.






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