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. 1972 Feb;1(2):107–111. doi: 10.1128/aac.1.2.107

Relation of β-Lactamase Activity and Cellular Location to Resistance of Enterobacter to Penicillins and Cephalosporins

Harold C Neu a,1, Elaine B Winshell a
PMCID: PMC444177  PMID: 4218941

Abstract

The Enterobacter species E. aerogenes, E. cloacae, and E. hafnia were examined for resistance to penicillin and cephalosporin derivatives. All were resistant to benzyl penicillin, ampicillin, 6 [d(−)α-amino-p-hydroxyphenylacetamido] penicillanic acid, cephaloridine, cephalothin, and cephalexin. A significant number were sensitive to carbenicillin and 6 [d(−)α-carboxy-3-thienylacetamido] penicillanic acid. No differences among the three species were noted. The β-lactamase activity was cell-bound, and was not released by osmotic shock, toluene treatment, or diphenylamine treatment. It was rarely released into the growth medium. The β-lactamase activity was primarily directed against cephalosporin derivatives. Synthesis of β-lactamase was chromosomally mediated. Resistance to ampicillin seemed to be partly related to entry of the molecule into the bacteria since exposure to ethylenediaminetetraacetate lowered the minimal inhibitory concentration.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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