The number of phage T2H particles decreased with an increase in the amounts of authentic D-arginine and the lipoprotein preparation from Escherichia coli B. The number of phage particles, preincubated with D-arginine or lipoprotein preparation, did not decrease with the addition of indole which inhibits the adsorption of phage T2H to the host cell. These results suggest that D-arginine defines the characteristics of the adsorption of phage T2H or occupies the determinant group of the receptor site for the phage on the cell surface of E. coli B.
The radioactivity of [^3H]-thymidine-labeled phage T2H DNA was coincident with the NADH oxidase activity in the inner membrane fraction from the cell envelope of E. coli B, by centrifugation in a sucrose density gradient. It is quite possible that the phage DNA which binds to the receptor site on lipoprotein moiety in the outer membrane may reach specific loci on the inner membrane within 20 min of a latent period, after which production of the phage virion would occur.