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The Journal of Immunology, 1972, 108: 748-754.
Copyright © 1972 by The American Association of Immunologists, Inc.
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Cell Surface Immunoglobulin

I. Isolation and Characterization of Immunoglobulin from Murine Mycloma Cells1

Sonia Baur2, Isaac Schenkein and Jonathan W. Uhr

Irvington House Institute and Department of Medicine, New York University School of Medicine, New York, New York 10016

Abstract

Enzymatic radioiodination has been used to investigate the cell surface of three murine myeloma tumors that secrete Ig. In each cell type studied (IgG1, IgG2a and IgA), radiolabeled Ig can be obtained from the cell surface by specific precipitation. In one cell line, surface IgG was also identified by digestion with trypsin followed by fingerprinting as well as by digestion with papain into characteristic Fab and Fc fragments. The Fc fragment contained a significant amount of radioactivity consistent with the concept that the IgG molecule is fully exteriorized. In each plasma cell line studied, Ig was associated with a molecular weight equal to or greater than 200,000 daltons which may be the complex between Ig and the molecule(s) on the plasma membrane to which it is attached.

Footnotes

1 This work was done under the sponsorship of the Commission on Immunization of the Armed Forces Epidemiological Board and was supported in part by the United States Army Medical Research Development Command, Department of the Army, under Research Contract DADA 17-69-C 9177, in part by United States Public Health Service Grant No. AI-0834, and by National Science Foundation Grant GB-7473-X.

2 Recipient of United States Public Health Service Special Fellowship 5 F03 AM35827-02.






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