| Abstract: | Two in vitro B cell tumor lines have been used to characterize and partially purify a lymphokine, or family of lymphokines, from monoclonal helper T cell immune response supernatants. These lymphokines induce the pre-B-like 70Z/3 tumor cell to synthesize Ig L chains and express complete Ig molecules on its cell surface, and cause the mature B cell-like WEHI-279 tumor cell to increase its ratio of secretory to membrane mu production, begin high rate Ig secretion, and then die. Most of the activity responsible for these changes co-purifies during five different separation procedures, implying the existence of a discrete molecule or closely related class of molecules able to mediate all of these effects. The molecules active in these systems appear distinct from the other lymphokines IL 1, IL 2, G/M-CSA, TRF, IFN, BCGF, and the activity variously termed IL 3/BPA/PSF/HCGF/MCGF, etc. We call these B cell-differentiating molecules BMF, or B cell maturation factor(s). The BMF molecules are mildly acidic (pI 5 to 6 in various conditions), extremely hydrophobic, probably heterogeneously glycosylated glycoproteins, with an apparent m.w. of 50,000 to 55,000 by gel permeation chromatography and 16,000 by SDS-PAGE. BMF has been purified approximately 3000-fold by three sequential chromatographic steps, with the use of the B tumor line assay systems. BMF molecules thus purified also cause normal resting splenic B cells to mature to the state of active Ig secretion. |
