The d-alanine carboxypeptidase was solubilized from the membranes of Bacillus subtilis with the nonionic detergent, Triton X-100, and purified to homogeneity. The purified protein bound irreversibly radioactivity from [14C]penicillin G. It contained a single polypeptide chain of molecular weight 50,000 and existed in solution as a protein-detergent aggregate of molecular weight about 350,000. The amino acid analysis did not indicate that the protein was unusually hydrophobic.
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Umbreit et al. (1973) studied this question.
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