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. 1974 Feb;117(2):783-5.
doi: 10.1128/jb.117.2.783-785.1974.

Inhibition of the Bacillus subtilis membrane-bound D-alanine carboxypeptidase by 6-aminopenicillanic acid covalently coupled to sepharose

D R Storm, P M Blumberg, J L Strominger

Inhibition of the Bacillus subtilis membrane-bound D-alanine carboxypeptidase by 6-aminopenicillanic acid covalently coupled to sepharose

D R Storm et al. J Bacteriol. 1974 Feb.

Abstract

An insoluble penicillin derivative, 6-aminopenicillanic acid covalently coupled to Sepharose, was used to investigate the location of the d-alanine carboxypeptidase in the Bacillus 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 the d-alanine carboxypeptidase exists on the outer face of the bacterial membrane.

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