Characterization of murine interleukin B by a monoclonal antibody

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Abstract
Interleukin B (IL-B) (ref. 1), formerly termed BEF (B-cell-derived enhancing factor)2,3 or IL-B4 (ref. 4), was originally described as a non-immunoglobulin regulatory factor spontaneously produced by B lymphocytes and B-cell lines that enhances the in vitro antigen-driven antibody response of unfractionated spleen cells stimulated by thymus-dependent antigens2,3. Since then we have examined the function of interleukin B in a number of immune reactions, both in vitro and in vivo5, and found that it inhibits the activation of suppressor T lymphocytes3,6–9. We report here the production of two monoclonal antibodies (mAb) that specifically inhibit interleukin B activity. The use of these mAb in the purification and characterization of IL-B is described. IL-B from both normal and transformed B cells consists of two subunits of similar size and amino-acid composition. The structure of interleukin B and its specific behaviour in biological assay distinguish it from many other known lymphokines.