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- W2004693530 abstract "Ten clinical isolates and the type strain (H37Rv) of Mycobacterium tuberculosis were shown to produce an intracellular β-lactamase. Crude enzyme preparations were extracted from acetone cell powders by grinding with zirconium beads in 0.133 M glycine with 1.0% Triton X-100. The enzymes had identical patterns on isoelectric focusing, with two major bands at isoelectric points of 4.9 and 5.1. The β-lactamase was highly susceptible to the new β-lactamase inhibitor BRL 42715, with an I50 of 0.0001 µg/ml. The enzyme was also susceptible to clavulanic acid with an I50 (0.05 µg/ml), which was similar to the value for the common bacterial β-lactamase TEM-1 (0.01 µg/ml). The latter result is consistent with previous MIC studies with M. tuberculosis, which have shown synergy between clavulanic acid and amoxicillin. BRL 42715 and clavulanic acid were more active than sulbactam, tazobactam, and cloxacillin. These studies support the potential value of penicillin/clavulanic acid and penicillin/BRL 42715 combinations in the treatment of tuberculosis." @default.
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- W2004693530 title "Beta-Lactamase Inhibitors and the Inducibility of the Beta-Lactamase ofMycobacterium tuberculosis" @default.
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- W2004693530 doi "https://doi.org/10.1164/ajrccm/145.3.657" @default.
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