THE NATURE OF THE BINDING OF PENICILLIN BY BACTERIAL CELLS

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Abstract
Alkaline extraction of cells of Micrococcus pvogenes treated with S35 penicillin resulted in destruction of the penicillin-cell complex. On the basis of several types of chromatographic evidence, the degradation product has been identified as penicilloic acid. The hypothesis has been proposed that binding occurs by cleavage of the beta-lactam ring of penicillin and combination of the carbonyl or the imino group of that ring with the binding component. Extraction of penicillin-bound cells with aqueous sodium lauryl sulfate yielded a material which, as far as could be determined, was the unchanged penicillin-cell complex. The material was for the most part dialyzable through cellophane and was not extracted into organic solvents at a neutral pH.