Abstract
Mast cells, basophils and a tumour analogue—rat basophilic leukaemia (RBL) cells—have a surface glycoprotein (Rε) which specifically binds monomeric immunoglobulin E (IgE)1, and aggregation of Rε causes secretion1–3. When isolated from non-ionic detergent extracts of surface-labelled RBL cells by IgE-specific immunoprecipitation, Rε appears as a 50,000 (50 K) to 60,000 (60 K) molecular weight (MW) band on electrophoresis in polyacrylamide gels in SDS (SDS-PAGE)4,5. Likewise, only a 50 K component is observed when the polypeptide that binds IgE is isolated by affinity chromatography in conditions which prevent aggregation of the IgE6–8, even when intrinsically labelled Rε is studied9. To determine how Rε is inserted into the plasma membrane, we reacted RBL cells with the photolysable hydrophobic reagent 5-iodonaphthyl-1-azide (INA), which preferentially labels the intramembranous segments of several intrinsic membrane proteins10,11. We report here that, surprisingly, the label was found, not on the 50 K glycopeptide, but only on a 30 K component which other studies suggest is a subunit of Rε (refs 9,12).
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Holowka, D., Gitler, C., Bercovici, T. et al. Reaction of 5-iodonaphthyl-1-nitrene with the IgE receptor on normal and tumour mast cells. Nature 289, 806–808 (1981). https://doi.org/10.1038/289806a0
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DOI: https://doi.org/10.1038/289806a0
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