The Journal of Experimental Medicine, Vol 132, 148-162,
Copyright © 1970 by The Rockefeller University Press
SYNTHESIS AND ASSEMBLY OF IMMUNOGLOBULINS BY MALIGNANT HUMAN PLASMACYTES
:
I. MYELOMAS PRODUCING 
-CHAINS AND LIGHT CHAINS
Susan Zolla Ph.D.1,
Joel Buxbaum M.D.1,
E. C. Franklin M.D.1, and
M. D. Scharff M.D.1
1 From the Department of Medicine, New York University Medical Center, New York 10016, and the Departments of Cell Biology and Medicine, Albert Einstein College of Medicine, Bronx, New York 10461
Three basic patterns of -globulin synthesis are described in malignant human plasmacytes: extreme unbalanced synthesis where only L chains are synthesized; unbalanced synthesis in which intact G globulin and an excess of free L chains are synthesized and secreted; and balanced synthesis where H and L chains appear to be synthesized in equimolar amounts. Studies of the cellular products appear to reflect the biosynthetic processes of the cells in a more reliable fashion than does analysis of serum or urinary proteins.
The absence of Bence Jones proteins from the urine does not necessarily indicate that free L chains are not being synthesized and secreted at the cellular level. Similarly, the completed globulin molecule secreted by malignant plasma cells may not be demonstrable by examination of serum.
Patterns of globulin synthesis in human myelomatous tissues vary as do patterns of globulin synthesis in mouse plasmacytomas.
Pulse-chase studies of the cells from one patient showed that a G myeloma protein was assembled via an HL (half molecule) intermediate.
Submitted on March 10, 1970
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