SUMMARY: Organisms (logarithmic growth phase) of strain 749/C when washed and resuspended in buffer ceased to produce penicillinase but continued to release their cell-bound enzyme as typical exopenicillinase. In the first 1-2 hr, 15-30% of the bound enzyme was liberated; the process then became very slow. Liberation was dependent upon temperature and pH value; it was not inhibited by chloramphenicol. Release was apparently not a result of membrane damage, since there was no leakage of intracellular α-glucosidase. Lysis of the bacilli decreased sharply the rate of release of coenzyme. Membrane preparations active in releasing penicillinase were obtained by lysing the bacilli with lysozyme in the absence of added Mg and subsequently adding 0.05 m-MgSO to prevent dispersal of the membrane segments. The liberation of penicillinase by this fraction had the same general enzymic properties as had the process with intact bacilli. Disruption of the membranes also eliminated most of the penicillinase-releasing activity. The importance of membrane structure in the liberation process is discussed.


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