Effect of Cephapirin on Formation of d -Alanine Carboxypeptidase in Growing Bacillus subtilis Cells
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چکیده
منابع مشابه
D=Alanine Carboxypeptidase from Bacillus subtilis Membranes
The D-alanine carboxypeptidase was solubilized from the membranes of Bacillus subtilis with the nonionic detergent, Triton X-100, and pursed to homogeneity. The purified protein bound irreversibly radioactivity from [Wlpenicillin 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 a...
متن کاملInactivation of D-alanine carboxypeptidase by penicillins and cephalosporins is not lethal in Bacillus subtilis.
The D-alanine carboxypeptidase of Bacillus subtilis is a particulate enzyme that is irreversibly inactivated by penicillins and cephalosporins. However, the lethal concentrations of these antibiotics are not the same as those that inhibit enzymatic activity in vitro. 6-Aminopenicillanic acid inactivates at least 95% of the enzyme at nonlethal concentrations. Conversely, cephalothin is lethal at...
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The D-alanine carboxypeptidase of B. subtilis is a membrane-bound enzyme which is inhibited by penicillins and binds them covalently. The enzyme has been labeled with [14C]- or [35S]penicillin. After tryptic or Pronase digestion of the labeled, denatured, reduced, and carboxymethylated enzyme, a radioactive peptide was isolated in each case. The amino acid compositions of these two peptides are...
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ژورنال
عنوان ژورنال: Antimicrobial Agents and Chemotherapy
سال: 1979
ISSN: 0066-4804,1098-6596
DOI: 10.1128/aac.15.2.204