Characterization of an Extended-Spectrum β-Lactamase from Escherichia coli Mediated by a Plasmid

Matsuhisa Inoue; Aisaku Fuse; Keizo Yamaguchi; Harushige Kanno; Mitsuo Kaku; Takashi Inamatsu; Tsutomu Nagahama; Masato Yoshida; Masato Nonoyama; Ryoichi Okamoto

doi:10.1007/BF02347732

Characterization of an Extended-Spectrum β-Lactamase from Escherichia coli Mediated by a Plasmid

Matsuhisa Inoue, Aisaku Fuse, Keizo Yamaguchi, Harushige Kanno, Mitsuo Kaku, Takashi Inamatsu, Tsutomu Nagahama, Masato Yoshida, Masato Nonoyama, Ryoichi Okamoto

MED - Medical Sciences

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

Abstract

The β-lactamase from Escherichia coli ML 4953 pKU56 was purified about 190-fold from the crude cell-free extract with an overall recovery of 17%. The molecular weight mediated by pKU56 was about 28,000, and the isoelectric point was about 9.4. This enzyme hydrolyzed cephaloridine, cephalothin, cefamandole, cefuroxime, and cefsulodin at high rate, but ampicillin, piperacillin, and carbenicillin moderately. Antisera against pKU56 enzyme showed partly cross-reaction with β-lactamase from Klebsiella oxytoca and Proteus vulgaris.

Original language	English
Pages (from-to)	70-72
Number of pages	3
Journal	Journal of Infection and Chemotherapy
Volume	1
Issue number	1
DOIs	https://doi.org/10.1007/BF02347732
Publication status	Published - 1995

Keywords

extended-spectrum
pKU56
β-lactamase

ASJC Scopus subject areas

Microbiology (medical)
Pharmacology (medical)
Infectious Diseases

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1007/BF02347732

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Characterization of an Extended-Spectrum β-Lactamase from Escherichia coli Mediated by a Plasmid. / Inoue, Matsuhisa; Fuse, Aisaku; Yamaguchi, Keizo; Kanno, Harushige; Kaku, Mitsuo; Inamatsu, Takashi; Nagahama, Tsutomu; Yoshida, Masato; Nonoyama, Masato; Okamoto, Ryoichi.

In: Journal of Infection and Chemotherapy, Vol. 1, No. 1, 1995, p. 70-72.

Research output: Contribution to journal › Article › peer-review

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title = "Characterization of an Extended-Spectrum β-Lactamase from Escherichia coli Mediated by a Plasmid",

abstract = "The β-lactamase from Escherichia coli ML 4953 pKU56 was purified about 190-fold from the crude cell-free extract with an overall recovery of 17%. The molecular weight mediated by pKU56 was about 28,000, and the isoelectric point was about 9.4. This enzyme hydrolyzed cephaloridine, cephalothin, cefamandole, cefuroxime, and cefsulodin at high rate, but ampicillin, piperacillin, and carbenicillin moderately. Antisera against pKU56 enzyme showed partly cross-reaction with β-lactamase from Klebsiella oxytoca and Proteus vulgaris.",

keywords = "extended-spectrum, pKU56, β-lactamase",

author = "Matsuhisa Inoue and Aisaku Fuse and Keizo Yamaguchi and Harushige Kanno and Mitsuo Kaku and Takashi Inamatsu and Tsutomu Nagahama and Masato Yoshida and Masato Nonoyama and Ryoichi Okamoto",

note = "Funding Information: This work was supported by grants 05304028 and 930050 from the Ministry of Education, Science and Culture, JapanWaksman Foundation, and the All Kitasato Project Study (6-2-3g).The following pharmaceutical companies kindly provided the drugs utilized in this study: Cefsulodin (Takeda Pharmaceutical, 'Osaka), cephaloridin, cephalothin, cephalexin, latamoxefand flomoxef( Shionogi Pharmaceutical, Osaka), piperacillin, cefoperazone (Toyama Chemical, Tokyo), cefoxitin (Daiichi Pharmaceutical, Tokyo), cefuroxime (Sinnihon Jit$ugyo,Tokyo), ceftazidime (Tanabe Pharmaceutical,Tokyo), ceftizoxime and carbepicillin (Fujisawa Pharmaceutical, Osaka), aztreonam (Eizai, Tokyo), cefotaxime and cefpirome (Hoechst,Tokyo), cefodizime and tazobactam (Taiho Pharmaceutical, Tokushima), clavulanic acid(Smith Klein Beecham Pharmaceutical,Tokyo), ampicillin (Meiji Seika, Tokyo), sulbactam (pfizer Pharmaceutical, Tokyo), and imipenem,penicillin G and cloxacillin (Banyu Pharmaceutical, Tokyo).",

year = "1995",

doi = "10.1007/BF02347732",

language = "English",

volume = "1",

pages = "70--72",

journal = "Journal of Infection and Chemotherapy",

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T1 - Characterization of an Extended-Spectrum β-Lactamase from Escherichia coli Mediated by a Plasmid

AU - Inoue, Matsuhisa

AU - Fuse, Aisaku

AU - Yamaguchi, Keizo

AU - Kanno, Harushige

AU - Kaku, Mitsuo

AU - Inamatsu, Takashi

AU - Nagahama, Tsutomu

AU - Yoshida, Masato

AU - Nonoyama, Masato

AU - Okamoto, Ryoichi

N1 - Funding Information: This work was supported by grants 05304028 and 930050 from the Ministry of Education, Science and Culture, JapanWaksman Foundation, and the All Kitasato Project Study (6-2-3g).The following pharmaceutical companies kindly provided the drugs utilized in this study: Cefsulodin (Takeda Pharmaceutical, 'Osaka), cephaloridin, cephalothin, cephalexin, latamoxefand flomoxef( Shionogi Pharmaceutical, Osaka), piperacillin, cefoperazone (Toyama Chemical, Tokyo), cefoxitin (Daiichi Pharmaceutical, Tokyo), cefuroxime (Sinnihon Jit$ugyo,Tokyo), ceftazidime (Tanabe Pharmaceutical,Tokyo), ceftizoxime and carbepicillin (Fujisawa Pharmaceutical, Osaka), aztreonam (Eizai, Tokyo), cefotaxime and cefpirome (Hoechst,Tokyo), cefodizime and tazobactam (Taiho Pharmaceutical, Tokushima), clavulanic acid(Smith Klein Beecham Pharmaceutical,Tokyo), ampicillin (Meiji Seika, Tokyo), sulbactam (pfizer Pharmaceutical, Tokyo), and imipenem,penicillin G and cloxacillin (Banyu Pharmaceutical, Tokyo).

PY - 1995

Y1 - 1995

N2 - The β-lactamase from Escherichia coli ML 4953 pKU56 was purified about 190-fold from the crude cell-free extract with an overall recovery of 17%. The molecular weight mediated by pKU56 was about 28,000, and the isoelectric point was about 9.4. This enzyme hydrolyzed cephaloridine, cephalothin, cefamandole, cefuroxime, and cefsulodin at high rate, but ampicillin, piperacillin, and carbenicillin moderately. Antisera against pKU56 enzyme showed partly cross-reaction with β-lactamase from Klebsiella oxytoca and Proteus vulgaris.

AB - The β-lactamase from Escherichia coli ML 4953 pKU56 was purified about 190-fold from the crude cell-free extract with an overall recovery of 17%. The molecular weight mediated by pKU56 was about 28,000, and the isoelectric point was about 9.4. This enzyme hydrolyzed cephaloridine, cephalothin, cefamandole, cefuroxime, and cefsulodin at high rate, but ampicillin, piperacillin, and carbenicillin moderately. Antisera against pKU56 enzyme showed partly cross-reaction with β-lactamase from Klebsiella oxytoca and Proteus vulgaris.

KW - extended-spectrum

KW - pKU56

KW - β-lactamase

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VL - 1

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JO - Journal of Infection and Chemotherapy

JF - Journal of Infection and Chemotherapy

SN - 1341-321X

IS - 1

ER -

Characterization of an Extended-Spectrum β-Lactamase from Escherichia coli Mediated by a Plasmid

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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