T
Tetsuo Sawai
Researcher at Chiba University
Publications - 107
Citations - 3395
Tetsuo Sawai is an academic researcher from Chiba University. The author has contributed to research in topics: Citrobacter freundii & Tetracycline transport. The author has an hindex of 31, co-authored 107 publications receiving 3330 citations. Previous affiliations of Tetsuo Sawai include Shinshu University & Gunma University.
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Journal ArticleDOI
Transport of divalent cations with tetracycline as mediated by the transposon Tn10-encoded tetracycline resistance protein.
TL;DR: The observation that 60Co2+ was actively taken up with tetracycline by the membrane vesicles prepared from resistant cells and inhibited in the presence of other divalent cations, indicating that these cations are also transported by a tetrACYcline resistance protein.
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Metal-tetracycline/H+ antiporter of Escherichia coli encoded by a transposon, Tn10. The role of the conserved dipeptide, Ser65-Asp66, in tetracycline transport.
TL;DR: Results indicate that a region including the dipeptide plays an important role in metal-tetracycline transport except for substrate binding, and may act as a gate which opens on the charge-charge interaction between Asp66 and the metal-TetracyCline.
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Drug resistance of enteric bacteria. XIV. Comparison of beta-lactamases in gram-negative rod bacteria resistant to alpha-aminobenzylpenicillin.
Tetsuo Sawai,Tetsuo Sawai,Susumu Mitsuhashi,Susumu Mitsuhashi,Saburo Yamagishi,Saburo Yamagishi +5 more
TL;DR: Results confirmed the stable existence of both factors in Shigella strains isolated from dysenteric patients, and the hetero-R state, where two types of R factor are found to exist stably in a host bacterium.
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The Purification and Properties of Penicillin β-Lactamases Mediated by Transmissible R Factors in Escherichia coli
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Amino Acid Substitutions in a Variant of IMP-1 Metallo-β-Lactamase
Shizuko Iyobe,Haruko Kusadokoro,Junko Ozaki,Naoki Matsumura,Shinzaburo Minami,Shin Haruta,Tetsuo Sawai,Koji O'Hara +7 more
TL;DR: The kinetic parameters indicated that extension of the substrate profile in the metallo-β-lactamase IMP-1 compared to IMP-3 is the result of a one-step single-base mutation, suggesting that the gene blaIMP- 3 is an ancestor ofblaIMp-1.