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

Abstract:

:The cell-surface component (alpha) which binds monomeric immunoglobulin E with high affinity is associated with a second polypeptide (beta) in the plasma membrane. The latter component tends to dissociate during purification of the alpha chain from detergent extracts of cells, even at neutral pHs and physiological ionic strengths. We now report that 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. These results suggest that 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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Rivnay B,Wank SA,Poy G,Metzger H

doi

10.1021/bi00269a047

subject

Has Abstract

pub_date

1982-12-21 00:00:00

pages

6922-7

issue

26

eissn

0006-2960

issn

1520-4995

journal_volume

21

pub_type

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