Purification and properties of dihydrostreptomycin-phosphorylating enzyme from Pseudomonas aeruginosa

KOBAYASHI Fujio, YAMAGUCHI Masahito, SATO Junko, MITSUHASHI Susumu

doi:10.1111/j.1348-0421.1972.tb00622.x

Purification and properties of dihydrostreptomycin-phosphorylating enzyme from Pseudomonas aeruginosa

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KOBAYASHI Fujio

Tokyo Research Laboralories, Kowa Co., Ltd. Department of Microbiology, School of Medicine, Gunma Universily
YAMAGUCHI Masahito

Tokyo Research Laboralories, Kowa Co., Ltd. Department of Microbiology, School of Medicine, Gunma Universily
SATO Junko

Tokyo Research Laboralories, Kowa Co., Ltd. Department of Microbiology, School of Medicine, Gunma Universily
MITSUHASHI Susumu

Tokyo Research Laboralories, Kowa Co., Ltd. Department of Microbiology, School of Medicine, Gunma Universily

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タイトル別名

Purification and Properties of Dihydrostreptomycin-Phosphorylating Enzyme from <i>Pseudomonas aeruginosa</i>
Purification and Properties of Dihydrostreptomyein‐Phosphorylating Enzyme from <i>Pseudomonas aeruginosa</i>

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説明

The distribution of the dihydrostreptomycin (DHSM)-phosphorylating enzyme was investigated using DHSM-resistant strains of Pseudomonas aeruginosa, indicating that this enzyme was demonstrated from all of 7 DHSM-resistant strains examined but not from a DHSM-sensitive one. The DHSM-phosphorylating enzyme was isolated from P. aeruginosa TI-13 and purified about 205-fold using Sephadex G-75 and DEAE-Sephadex A-50 column chromatography. The optimal pH for the DHSM-inactivation was around 10.0. and both adenosinetriphosphate (ATP) and Mg⁺⁺ were required for the inactivating reaction. It was found that this cnzyme inactivated only DHSM but not other aminoglycosidic antibioties such as kanamycin, aminodeoxykanamycin, neomycin, paromomycin, lividomycin and gentamicin.