Phospholipids stabilize the interaction between the .alpha. and .beta. subunits of the solubilized receptor for immunoglobulin E

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Abstract
The cell-surface component (.alpha.) which binds monomeric IgE with high affinity is associated with a 2nd polypeptide (.beta.) in the plasma membrane of rat basophilic leukemia RBL cells. The latter component tends to dissociate during purification of the .alpha. chain from detergent extracts of cells, even at neutral pH and physiological ionic strengths. The interaction of .alpha. and .beta. can be stabilized by maintaining an appropriate phospholipid to detergent ratio. Under such conditions, other discrete components reproducibly copurify with the .alpha. and .beta. chains. The subunits of this membrane protein-or the interaction of it with other constituents in the cell-may be stabilized in ways not observed with ordinary soluble proteins.