Purification and Properties of Dihydrostreptomycin-Phosphorylating Enzyme from Pseudomonas aeruginosa

Fujio KOBAYASHI; Masahito YAMAGUCHI; Junko SATO; Susumu MITSUHASHI

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

Purification and Properties of Dihydrostreptomycin-Phosphorylating Enzyme from Pseudomonas aeruginosa

Fujio KOBAYASHI, Masahito YAMAGUCHI, Junko SATO, Susumu MITSUHASHI

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JOURNAL FREE ACCESS

1972 Volume 16 Issue 1 Pages 15-19

DOI https://doi.org/10.1111/j.1348-0421.1972.tb00622.x

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Published: 1972 Received: August 16, 1971 Available on J-STAGE: April 18, 2008 Accepted: - Advance online publication: - Revised: -
Correction information
Date of correction: April 18, 2008 Reason for correction: - Correction: ABSTRACT Details: Wrong : The distribution of the dihydrostreptomycin (DHSM)-phosphorylating enzyme was investi-
gated 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, aminodeoxykana-
mycin, neomycin, paromomycin, lividomycin and gentamicin.
Right : 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.

Date of correction: April 18, 2008 Reason for correction: - Correction: AUTHOR Details: Wrong : Fujio KOBAYASHI¹⁾, Masahito YAMAGUCHI¹⁾, Junko SATO¹⁾, Susumu MITSUHASHI¹⁾
Right : Fujio KOBAYASHI¹⁾²⁾, Masahito YAMAGUCHI¹⁾²⁾, Junko SATO¹⁾²⁾, Susumu MITSUHASHI¹⁾²⁾

Date of correction: April 18, 2008 Reason for correction: - Correction: AFFILIATION Details: Wrong :
1) Tokyo Research Laboralories, Kowa Co., Ltd., Higashimurayama, Tokyo, and Department of

Right :
1) Tokyo Research Laboralories, Kowa Co., Ltd.
2) Department of Microbiology, School of Medicine, Gunma Universily

Date of correction: April 18, 2008 Reason for correction: - Correction: PDF FILE Details: -

Abstract

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.

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