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An insoluble penicillin derivative, 6-aminopenicillanic acid covalently coupled to Sepharose, was used to investigate the location of thed -alanine carboxypeptidase in theBacillus subtilis membrane. Only 50% of the enzymatic activity in protoplasts and 74% of that in purified membranes was sensitive, although the purified enzyme could be inhibited completely by the resin. These results suggest that a minimum of 50% of thed -alanine carboxypeptidase exists on the outer face of the bacterial membrane.

journal of bacteriology

Inhibition of the <i>Bacillus subtilis</i> Membrane-Bound <scp>d</scp> -Alanine Carboxypeptidase by 6-Aminopenicillanic Acid Covalently Coupled to Sepharose

Inhibition of the Bacillus subtilis Membrane-Bound d -Alanine Carboxypeptidase by 6-Aminopenicillanic Acid Covalently Coupled to Sepharose