EVALUATION OF THE β-LACTAMASE-STABILITY OF L-105 TO VARIOUS TYPES OF ENZYMES
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The stability of L-105 to β-lactamases was evaluated in nine groups of gram-negative bacteria which composed of constitutive producers of four kinds of penicillinases and five kinds of cephalosporinases, by means of inhibitory concentrations measured for the set of bacterial strains. Furthermore, the V<SUB>max</SUB> and Km values of seven of the nine β-lactamases for L-105 were determined with purified enzyme preparations. The obtained results were summarized as follows:<BR>1. L-105 showed low MIC values against all the penicillinase-producing bacteria tested and the MIC values were little affected by the penicillinase production in bacterial cells, suggesting excellent stability of L-105 to penicillinases. In the case of cephalosporinase-producing bacteria, the MIC values against high enzyme producers were somewhat higher than those against lower producers, but the highest MIC was 6.3 μg per ml.<BR>2. L-105 was hydrolyzed by <I>Proteus vulgaris</I> cephalosporinase (cefroxime-hydrolyzing enzyme) at the highest rate among the seven purified β-lactamases tested, but the hydrolysis rate was onefifth that of the cephaloridine-hydrolysis. L-105 showed high stability to six other β-lactamases, especially to common cephalosporinases.<BR>3. The affinity of the seven β-lactamases with L-105 was high in comparison with cephaloridine, and the Km values were distributed among 0.3 to 28 μM.<BR>4. The kinetic behavior of the β-lactamases toward L-105 was similar to that toward cefmenoxime, an analogue of L-105.
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公益社団法人 日本化学療法学会 | 論文
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