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

Research output: Contribution to journalArticlepeer-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 languageEnglish
Pages (from-to)70-72
Number of pages3
JournalJournal of Infection and Chemotherapy
Volume1
Issue number1
DOIs
Publication statusPublished - 1995 Jan 1

Keywords

  • extended-spectrum
  • pKU56
  • β-lactamase

ASJC Scopus subject areas

  • Microbiology (medical)
  • Pharmacology (medical)
  • Infectious Diseases

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