Nonspecific Ionic Inhibition of Ethambutol Binding by Mycobacterium smegmatis
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چکیده
منابع مشابه
Nonspecific ionic inhibition of ethambutol binding by Mycobacterium smegmatis.
Magnesium sulfate and spermidine were tested for their effects on binding of (14)C-ethambutol by Mycobacterium smegmatis. Concentrations were used that protected the organism from ethambutol inhibition. Sodium salts were examined as possible ethambutol antagonists to test the previously reported specificity of the divalent cation salt effect. Consistent with growth-protection experiments, 20 mM...
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Polyamines protected Mycobacterium smegmatis from ethambutol inhibition but not from streptomycin inhibition, whereas MgSO(4) neutralized growth inhibition by both drugs.
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Mycobacterium smegmatis PTCC 1307 (CIP 73.26) was used as a microbial agent to produce androsta-1,4-diene-3,17-dione (ADD) and androst-4-ene-3,17-dione, two useful precursors in the synthesis of steroid drugs. The side chain of cholesterol, as the substrate, was selectively cleaved in the presence of five enzyme inhibitors. An intermediate structure with intact side chain, cholest-4-ene-3-one, ...
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Gale, Glen R. (Veterans Administration Hospital, Durham, N.C.) and Helen H. McLain. Effect of ethambutol on cytology of Mycobacterium smegmatis. J. Bacteriol. 86:749-756. 1963.-Electron microscopy showed the effects of the antimycobacterial drug, ethambutol [d-2,2'-(ethylenediimino)-di-1-butanol], on the cytology of Mycobacterium smegmatis. After 10 hr of exposure to the drug, cells no longer c...
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DNA topoisomerase I from Mycobacterium smegmatis unlike many other type I topoisomerases is a site specific DNA binding protein. We have investigated the sequence specific DNA binding characteristics of the enzyme using specific oligonucleotides of varied length. DNA binding, oligonucleotide competition and covalent complex assays show that the substrate length requirement for interaction is mu...
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ژورنال
عنوان ژورنال: Antimicrobial Agents and Chemotherapy
سال: 1973
ISSN: 0066-4804,1098-6596
DOI: 10.1128/aac.4.2.115