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
Biochemistryjournal_title
Biochemistryauthors
Rivnay B,Wank SA,Poy G,Metzger Hdoi
10.1021/bi00269a047subject
Has Abstractpub_date
1982-12-21 00:00:00pages
6922-7issue
26eissn
0006-2960issn
1520-4995journal_volume
21pub_type
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