STABILITY AGAINST β-LACTAMASES AND AFFINITIES FOR PENICILLIN-BINDING PROTEINS OF 7432-S, A NEW ORAL CEPHALOSPORIN
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A new oral cephalosporin, 7432-S, which has a carboxyethylidene substituent at the 7 position, was stable against both penicillinases of Gram-negative bacteria and those mediated by R plasmids. 7432-S showed high affinity for various cephalosporinases except the enzyme from Proteus, uulgaris but their Vmax values remained very low.<BR>The β-lactamase from <I>Bacteroides fragilis</I> however, hydrolysed 7432-S.<BR>7432-S bound specifically to the penicillin-binding protein 3 (PBP-3) of <I>Escherichia coli</I> K12 and <I>P. vulgaris</I> CN329 and its ID<SUB>50</SUB> values correlated to the MICs, but it showed low affinity for the other PBPs. 7432-S had poor affinity for PBPs-2 and-3 of <I>Staphylococcus aureus</I> ATCC 25923, which represented the lethal targets. This explains its weak anti-taphylococcal activity.
- 公益社団法人 日本化学療法学会の論文
公益社団法人 日本化学療法学会 | 論文
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