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. 1975 Apr;147(1):131-7.
doi: 10.1042/bj1470131.

Purification of D-alanine carboxypeptidase from Escherichia coli B on a penicillin-Sepharose column

M Gorecki, A Bar-Eli, Y Burstein, A Patchornik, E B Chain

Purification of D-alanine carboxypeptidase from Escherichia coli B on a penicillin-Sepharose column

M Gorecki et al. Biochem J. 1975 Apr.

Abstract

1. A soluble D-alanine carboxypeptidase from Escherichia coli strain B was purified on a p-aminobenzylpenicillin-Sepharose column. This one-step chromatography followed by an (NH4)2SO4 precipitation yielded an enzyme purified 1200-fold and some of its properties are reported. 2. The pure D-alanine carboxypeptidase was devoid of D-alanine carboxypeptidase II activity and migrated as a single protein band on analytical disc gel electrophoresis. 3. Triton X-100 in the purification procedure is an absolute requirement for obtaining a stable enzyme. 4. The enzymic activity of D-alanine carboxypeptidase was greatly affected in solution of high salt concentrations and varied somewhat with the nature of the cation tested.

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