SUMMARY: The properties (Michaelis constants, rates of inactivation at 100°, temperature coefficients and pH/activity relationships) of the extracellular penicillinase formed by a strain of when growing in casein hydrolysate (= ‘basal’ enzyme) have been compared with those of the enzyme formed by the organism when growing in the same medium after addition of 1 unit benzylpenicillin/ml. (= ‘induced’ enzyme); no differences between the two preparations were detected. Similarly, no immunological or other differences were found between the basal and induced penicillinases of , strain 569. However, the penicillinase was significantly different from the penicillinase in the value of its Michaelis constant and the shape of its pH/activity curve; it was also quite distinct immunologically.


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