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Streptomycin-3"-phosphotransferases were isolated and purified from E. coli cells containing plasmids 836, pBS52 or R6K, which determine the microorganisms resistance towards streptomycin and dihydrostreptomycin. Phosphorylation of the 3"-hydroxylic group of dihydrostreptomycin was demonstrated by [13C]-NMR spectrometry. It was shown that streptomycin-3"-phosphotransferase, whose synthesis is determined by plasmid 836 (as well as by plasmid R6K), differs from the analogous enzyme, whose synthesis is operated by plasmid pBS52 in some properties, e. g. dependence of the initial reaction rate on concentrations of antibiotics and ATP, pH-optimum, sensitivity to the buffer ionic strength, stability, etc. Besides, the antiserum against streptomycin-3'-phosphotransferase detected by plasmid pBS52 does not produce cross immunological reactions with the other enzyme.
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