1973 Volume 19 Issue 3 Pages 209-219
1) Pyocin R-sensitive cells were digested with lysozyme in the presence of EDTA in hypertonic solution. Most of the receptor activity was solubilized, by this procedure, and separated from spheroplast membrane fraction. This suggested the location of receptor on the cell wall.
2) Electron microscopic figure revealed the adsorption of pyocin R on the cell surface and its fragment. Pyocin particles were adsorbed on the receptor site with the contracted sheath, at the tip of core.
3) Properties of interaction between pyocin R and its receptor were studied. Pyocin R inactivation by its adsorption to the receptor was highly dependent on temperature, and the presence of 0.1-0.2M NaCl was necessary for the optimal inactivation.
4) Size of receptor site required for the inactivation of a pyocin particle was estimated.