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The Journal of Immunology, 1979, 122: 1972-1977.
Copyright © 1979 by The American Association of Immunologists, Inc.

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Murine Plasma Cells Secreting More Than One Class of Immunoglobulin

VI. Secretion of Completely Assembled IgG2b and IgA Molecules with Segregated Heavy Chains and Free Light Chains by Spontaneous Myeloma SAMM 368 in Culture

Paul E. Mckeever, Mirdza E. Neiders1, Gregory B. Nero and Richard Asofsky

From the Laboratory of Microbial Immunity, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20205

Abstract

The antigenic and molecular characteristics of the two immunoglobulins secreted by a single cell line of plasmacytoma SAMM 368 were analyzed by polyacrylamide gel electrophoresis of biosynthesized proteins. Adapted to continuous in vitro cultivation, this BALB/c plasmacytoma secretes at least 98% of its heavy chains as components of fully assembled and isotypically uniform IgG2b and IgA molecules. The IgA is secreted as monomers, dimers, and multimers with chemical properties typical of BALB/c myeloma IgA including disulfide bonded J chain and noncovalently bonded light chains. The noncovalently bonded light chains are monomers rather than dimers. Free light chains are also secreted. The ability to segregate heavy chains is attributed either to chemical, enzymatic, or compartmental regulatory factors operating within these plasma cells.

Footnotes

1 Present address: Department of Oral Pathology, School of Dentistry, SUNY at Buffalo, Buffalo, New York 14214.







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