SUMMARY: The cell-bound penicillinase of strain 749/c was examined since this material appears to be an intermediate in the formation of the exopenicillinase. The enzyme remained attached to fragments of the cell membrane during lysis of the cell. It was not released from these fragments by a variety of physical or chemical treatments (urea, hydroxylamine, deoxycholate, ultrasound, etc.). Free penicillinase, very similar if not identical, to the exoenzyme, was produced by treatment with trypsin, proteinase or papain, but not by chymotrypsin, lipases or nucleases. The cell-bound enzyme appeared to be covalently linked to the cell membrane through a peptide chain. Trypsin probably cleaved this chain at a linkage involving the carboxyl group of lysine or arginine. The enzymic characteristics of the bound penicillinase are essentially equivalent to those of the exoenzyme. Partial purification of the membrane-bound enzyme is described.


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