Abstract
The reaction between penicillin and the penicillinase of Bacillus subtilis strain 749 C, in the cell-bound and the free states, was studied over the range pH 3.9-9.0. The results suggested that the bound penicillinase behaved as though it were reacting in an environment of significantly lower pH value than that of the bulk phase. This effect was not as great as that calculated from electrokinetic data for B. subtilis surfaces. Various ways of interpreting the data are discussed.

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