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Purification and Properties of Dihydrostreptomyein‐Phosphorylating Enzyme from Pseudomonas aeruginosa
Author(s) -
Kobayashi Fujio,
Yamaguchi Masahito,
Sato Junko,
Mitsuhashi Susumu
Publication year - 1972
Publication title -
japanese journal of microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0021-5139
DOI - 10.1111/j.1348-0421.1972.tb00622.x
Subject(s) - pseudomonas aeruginosa , dihydrostreptomycin , enzyme , chemistry , neomycin , sephadex , gentamicin , paromomycin , microbiology and biotechnology , sisomicin , aminoglycoside , antibiotics , biochemistry , chromatography , biology , bacteria , tobramycin , streptomycin , genetics
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 enzyme inactivated only DHSM but not other aminoglycosidic antibiotics such as kanamycin, aminodeoxykanamycin, neomycin, paromomycin, lividomycin and gentamicin.