Abstract
Leukocyte samples of 16 atopic and 14 non-atopic children were enriched in their basophils by single step Ficoll-Paque centrifugation to a relative concentration of 10-15% (Miroli, et al. 1986). Aliquots from each of these basophil preparations were incubated with the following monoclonal antibodies (mAbs): F4 and H10 shown previously to be specific for the high-affinity Fcε receptor present on the RBL-2K3 cells; G63 which recognizes a membrane protein different from the Fcε receptor and shown to cause inhibition of IgE mediated degranulation of RBL cells; B17 specific for a glycolipid present in the plasma membrane of RBL-2H3 cells end modulates their degranulation. In addition a monoclonal murine IgE was used to probe the occupancy of Fcε receptors. Following incubation, the binding of the mAbs was monitored by fluorescently labeled rabbit anti-mouse antibodies and the samples were analysed by the Fluorescence Activated Cell Sorter (FACS 440). The results show that all four mAbs also bind, though to different extents, to partially purified human basophils of both atopic and non-atopic children.
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Geller-Bernsteln, C., Berebi, A., Ortega, E. et al. 63 CROSS RERCTIVITY WITH HUMAN BRSOPHILS OF MONOCLINAL, ANTIBODIES RAISED AGAINST MEMBRANE COMPONENTS OF RAT MAST CELLS OF THE RBL-2H3 LINE. Pediatr Res 24, 271 (1988). https://doi.org/10.1203/00006450-198808000-00089
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DOI: https://doi.org/10.1203/00006450-198808000-00089