Abstract
The effect of the carboxylic ionophore, monensin, on the synthesis and expression of membrane IgM in the human lymphobiastoid cell line, Daudi, was investigated. The normal processing events in the maturation of μ chains and K chains were altered in monensin treated Daudi cells; the immunoglobuli n chains did not appear to undergo complete terminal glycosylation modifications. Transport of the glycoprotein to the plasma membrane could be demonstrated indicating that the interference of intracellular processing of the IgM by monensin did not significantly influence the membrane expression of the IgM.
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