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. 1969 Jun;17(6):783–786. doi: 10.1128/am.17.6.783-786.1969

Effect of β-Lactamase Location in Escherichia coli on Penicillin Synergy

Harold C Neu 1
PMCID: PMC377810  PMID: 4894721

Abstract

Resistance to ampicillin in Escherichia coli is due generally to the presence of a β-lactamase (penicillinase). Resistant strains have been found to fall into two groups: those with high-level resistance (1,000 μg/ml or greater) and those with low-level resistance (8 to 250 μg/ml). Most of the high-level resistant organisms posses β-lactamases whose synthesis is episomally mediated. These strains release penicillinase from the cell when they are subjected to osmotic shock. Low-level resistant strains do not release the enzyme with osmotic shock. High-level resistant strains are not susceptible to the synergistic action of a penicillinase-resistant penicillin with ampicillin. Seventy eight per cent of low-level resistant strains are susceptible to the synergistic action of ampicillin and oxacillin. The two types of β-lactamases are similar in regard to most properties; both enzymes are subject to competitive inhibition by penicillinase-resistant penicillins. The difference in location in the cell might explain why only some strains of E. coli are susceptible to the synergistic action of penicillin combinations.

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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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