Abstract
A trichloroacetic acid (TCA)-soluble fraction, extracted using cold TCA, was derived from the cell wall of Lactobacillus casei strain S-1. It not only inhibited the adsorption of phage J-1 but also de-orbed these phages, in their active form, which had previously been adsorbed onto the cell walls. L-Rhamnose, one of the components of this TCA-soluble fraction, had an identical activity to this TCA-soluble fraction, on phage adsorption. This suggested that L-rhamnose is a part of phage receptor material in the cell wall of L, casei strain S-1; and the binding of the phage to the cell wall is reversible, even at 37C.
