Abstract
A thermostable protein that strongly inhibits the soluble E. coli D-alanine carboxypeptidase was isolated from a cell-free extract of E. coli B . The inhibitor was purified 140-fold by heat treatment, selective precipitation at pH 4.5, ion exchange chromatography on DEAE-cellulose and gel chromatography on Sephadex G-100. Inhibition of soluble D-alanine carboxypeptidase by this inhibitor is reversed by cations such as Mg ++ or Na + and abolished by digestion of the inhibitor with proteolytic enzymes. The inhibitor does not affect either the particulate D-alanine carboxypeptidase of E. coli or the growth of the bacteria.
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