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Abstract
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 Bacillus subtilis 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 B. cereus, strain 569. However, the B. subtilis penicillinase was significantly different from the B. cereus 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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