It was shown that a chloramphenicol-resistant E. Search for related content. Abstract The chloramphenicol-inactivating enzyme in the multiple drug-resistant Escherichia coli carrying R factor produced two products from chloramphenicol in a cell-free system as well as in whole cells.
Related Content Load related web page information. Both purified preparations consist of native enzymes with molecular weights of 80, and evidence is presented that is consistent with their being made up of four identical subunits of 20, each.
User Name Password Sign In. These products were identified as d - thero dichloroacetamido p -nitrophenyl hydroxyacetoxypropane and d - threo dichloroacetamido p -nitrophenyl -1,3-diacetoxypropane. Studies of the substrate specificity, heat stability, pH optimum, and chromatographic behavior of the chloramphenicol-acetylating enzyme from the multiple drug-resistant E.
Responses Submit a Letter to the Editor. ABSTRACT The mechanism of chloramphenicol resistance in several multiple-resistant Staphylococcus epidermidis strains has been studied and shown to be due to the presence of the enzyme, chloramphenicol acetyltransferase. Bentley 2 and L. You'll be in good company. When the multiple drug-resistant E.
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Classifications Genetics and Molecular Biology. The mechanism of chloramphenicol resistance in several multiple-resistant Staphylococcus epidermidis strains has been studied and shown to be due to the presence of the enzyme, chloramphenicol acetyltransferase.
The chloramphenicol acetylating enzyme from S. Prev Next Table of Contents.
Related Content Load related web page information. The chloramphenicol-acetylating enzyme from the multiple drug-resistant E. The two staphylococcal enzymes are identical with respect to p H optimum, apparent affinity K m for chloramphenicol, heat denaturation, and immunological reactivity, but they differ in electrophoretic mobility, chromatographic behavior, substrate specificity, and sensitivity to inhibition by mercuric ion.
Alert me to new issues of JB. Shaw 1D. Articles by Sands, L. For an alternate route to JB. Google Scholar Articles by Suzuki, Y. It was not possible to decide whether one or two enzymes participate in the acetylation of chloramphenicol.