SUMMARY: Streptomycin 6-kinase of the streptomycin-producing strain HUT 6037 was purified by fractionation with (NH)SO and chromatography on DEAE-Sephadex A-25, hydroxyapatite and Sephadex G-100. After PAGE of the final fraction, a protein band corresponding to streptomycin 6-kinase was detected, together with a less intense band having no enzyme activity. Molecular weights determined by SDS-PAGE and by Sephadex G-100 chromatography were about 36000 and 38000, respectively, suggesting that the enzyme was a monomer. The isoelectric point of the enzyme was pH 6.6. Among the nucleoside 5′-triphosphates tested, ATP was the preferred phosphoryl donor. The K values for streptomycin and ATP were 3.5 mM and 0-4 mM, respectively. The enzyme activity was strongly inhibited by EDTA and ANO. It was shown by using an protein-synthesizing system that purified streptomycin 6-kinase could protect polyphenylalanine synthesis of the streptomycin-susceptible strain KSN from inhibition by streptomycin.


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