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. 1991 Feb;35(2):371–372. doi: 10.1128/aac.35.2.371

Biochemical properties and purification of metallo-beta-lactamase from Bacteroides fragilis.

K Bandoh 1, Y Muto 1, K Watanabe 1, N Katoh 1, K Ueno 1
PMCID: PMC245008  PMID: 1902649

Abstract

The beta-lactamase from Bacteroides fragilis GAI-30144 hydrolyzed imipenem, oxyiminocephalosporins, cephamycins, and penicillins. Enzyme activity was inhibited by EDTA. Zinc completely reversed inactivation of the enzyme by EDTA. The molecular mass of purified enzyme was estimated to be 33,000 daltons.

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Selected References

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