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The Journal of Immunology, 1973, 111: 448-456.
Copyright © 1973 by The American Association of Immunologists, Inc.

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Synthesis, Assembly and Secretion of {gamma}-Globulin by Mouse Myeloma Cells

V. Balanced and Unbalanced Synthesis of Heavy and Light Chains by IgG-Producing Tumors and Cell Lines1

Reuben Baumal2 and Matthew D. Scharff3

From the Department of Immunology, Sick Children's Hospital, Toronto, Canada, and the Departments of Cell Biology and Medicine, Albert Einstein College of Medicine, Bronx, New York 10461

Abstract

Normal lymphoid cells obtained from hyperimmunized BALB/c mice and cells from most but not all IgG-producing mouse myeloma tumors and cell lines synthesized more light (L) than heavy (H) chains. While most myeloma tumors secreted their excess L chains, two tumors, MOPC 21 and MOPC 173, degraded the excess L chains and did not secrete them. A third group of tumors produced the same number of H and L chains. In the case of the MPC-11 tumor, excess L chains were synthesized by cloned tumors and cell lines.

Footnotes

1 This work was supported by the Medical Research Council of Canada, the National Institutes of Health (AI 5231, AI 10702), the NSF (GB 3369), and the American Cancer Society.

2 Dr. Baumal is a scholar of the Medical Research Council of Canada.

3 Dr. Scharff is the recipient of an National Institutes of Health Career Development Award.

Requests for reprints should be addressed to Dr. R. Baumal, Department of Immunology, Sick Children's Hospital, 555 University Avenue, Toronto, Ontario, Canada.




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Covalent immunoglobulin assembly in vitro: reactivity of light chain covalent dimers (L2) and blocked light chain monomers
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R. Baumal, B. K. Birshtein, P. Coffino, and M. D. Scharff
Mutations in Immunoglobulin-Producing Moose Myeloma Cells
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