Phage 3 receptor substance was isolated from the plasma membrane of , strain 3, by extraction with sodium deoxycholate at 37°. A twelvefold purification of the receptor substance was obtained by filtering the deoxycholate extract through a column of Sepharose 4B, in the presence of deoxycholate. Receptor activity was specific for phage 3 and was associated with a lipoprotein fraction which contained five principal and some minor polypeptide components. When phage receptor substance was aged in the absence of deoxycholate, aggregation of lipoprotein and a reversible loss of receptor substance occurred. Receptor activity was destroyed by extraction of the receptor substance with ether + ethanol at -20° and was decreased by incubation with trypsin. Activity was not affected by oxidation with sodium periodate or by digestion with lipase or phospholipases. The phage receptor substance was precipitated by antibody to the plasma membrane and activity appeared to be confined to a small proportion of the antigenic lipoprotein molecules.


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