Nippon Saikingaku Zasshi
Online ISSN : 1882-4110
Print ISSN : 0021-4930
ISSN-L : 0021-4930
Volume 47, Issue 2
Displaying 1-8 of 8 articles from this issue
  • Osamu KOHASHI
    1992 Volume 47 Issue 2 Pages 353-365
    Published: March 25, 1992
    Released on J-STAGE: February 19, 2009
    JOURNAL FREE ACCESS
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  • Masatoshi NODA
    1992 Volume 47 Issue 2 Pages 367-372
    Published: March 25, 1992
    Released on J-STAGE: February 19, 2009
    JOURNAL FREE ACCESS
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  • Chieko JIN
    1992 Volume 47 Issue 2 Pages 373-385
    Published: March 25, 1992
    Released on J-STAGE: February 19, 2009
    JOURNAL FREE ACCESS
    The β-lactam resistance of genus Streptococcus has been explained by the low binding affinity of penicillin-binding proteins (PBPs) to the drug.
    This study was carried out to resolve the mechanisms of resistance to β-lactam antibiotics in the species of genus Enterococcus by means of binding affinities of PBPs. Streptococcus pyogenes, Enterococcus faecalis, Enterococcus faecium and Enterococcus avium were employed as assay microbes.
    Cefepime (CFPM) and ampicillin (ABPC) were used as representatives of cephems and penicillins, respectively.
    All the PBP fractions of S. pyogenes manifested high binding affinities to CFPM and ABPC, whereas PBPs 1 and 4 of E. faecalis showed high binding affinities to ABPC but not to CFPM.
    In E. faecium, PBPs of an exceptionally penicillin-susceptible strain manifested a high binding affinity to ABPC, but PBPs 5 and 6 showed low affinities to CFPM. β-lactam resistant strains of E. faecium possessed PBPs 5 and 6 with low binding affinities to CFPM and ABPC.
    All the fractions of PBPs but PBP 1 in E. avium showed low binding affinities to CFPM. Although all the PBP fractions but PBPs 3 and 6 manifested high binding affinities to ABPC, PBPs 3 and 6 showed low binding affinities to ABPC. A strain of E. avium, which is susceptible to ABPC but moderately resistant to CFPM, lacked PBP 6.
    In conclusion, the resistance of E. avium to CFPM is based upon low binding affinities of the many fractions to this drug, and ABPC resistance is based upon PBPs 3 and 6 with low binding affinities to ABPC.
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  • Yukiko GOHARA, Sumio ARAI, Koichi KUWANO, Takanori KAWASHIMA, Ikuko MA ...
    1992 Volume 47 Issue 2 Pages 387-393
    Published: March 25, 1992
    Released on J-STAGE: February 19, 2009
    JOURNAL FREE ACCESS
    The antimicrobial activities against Mycoplasma pneumoniae of new quinolones (temafloxacin, ofloxacin, ciprofloxacin, enoxacin, and norfloxacin) and of tetracyclines and macrolides as controls were compared. Among new quinolones, temafloxacin, ofloxacin, and ciprofloxacin were more active than enoxacin and norfloxacin against fifty strains of Mycoplasma pneumoniae, giving MIC50 and MIC90 significantly lower than those of the latter two, by the agar-dilution method. The three more active antibiotics in the above assay were then determined for MICs and MBCs by the broth-dilution method. The MICs of every antibiotic except erythromycin determined by both the methods were very similar each other. The MICs of erythromycin determined by the broth-dilution method were ten-times higher than those determined by the agar-dilution method. temafloxacin and ofloxacin gave MBCs only about four-times higher than MICs, whereas ciprofloxacin, minocycline, erythromycin and josamycin gave MBCs as much as 15 to 1, 000-times higher than MICs. From the MICs and MBCs determined by the two assay methods, it is apparent that temafloxacin and ofloxacin, and to a less extent ciprofloxacin, have more potent mycoplasmacidal activities than do macrolides and tetracyclines.
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  • Hiroto SHINOMIYA, Shinji SAITO
    1992 Volume 47 Issue 2 Pages 395-402
    Published: March 25, 1992
    Released on J-STAGE: February 19, 2009
    JOURNAL FREE ACCESS
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  • 1992 Volume 47 Issue 2 Pages 403-418
    Published: March 25, 1992
    Released on J-STAGE: February 19, 2009
    JOURNAL FREE ACCESS
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  • 1992 Volume 47 Issue 2 Pages 419-434
    Published: March 25, 1992
    Released on J-STAGE: February 19, 2009
    JOURNAL FREE ACCESS
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  • 1992 Volume 47 Issue 2 Pages 435-454
    Published: March 25, 1992
    Released on J-STAGE: February 19, 2009
    JOURNAL FREE ACCESS
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