Nippon Saikingaku Zasshi
Online ISSN : 1882-4110
Print ISSN : 0021-4930
ISSN-L : 0021-4930
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Volume 39, Issue 6
Displaying 1-5 of 5 articles from this issue
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  • Studies on immune bactericidal reaction
    Kozo INOUE
    1984 Volume 39 Issue 6 Pages 833-848
    Published: November 25, 1984
    Released on J-STAGE: February 19, 2009
    DOIhttps://doi.org/10.3412/jsb.39.833
    JOURNAL FREE ACCESS
    Download PDF (8552K)
  • Studies on pseudomonal and staphylococcal leukocidins
    Toshiya HIRAYAMA, Masatoshi NODA
    1984 Volume 39 Issue 6 Pages 849-863
    Published: November 25, 1984
    Released on J-STAGE: February 19, 2009
    DOIhttps://doi.org/10.3412/jsb.39.849
    JOURNAL FREE ACCESS
    Download PDF (14628K)
  • Establishment of an Experimental System of Macrophage Cell Lines Obtained by SV40 Transformation
    Atsushi TAKAGI
    1984 Volume 39 Issue 6 Pages 865-868
    Published: November 25, 1984
    Released on J-STAGE: February 19, 2009
    DOIhttps://doi.org/10.3412/jsb.39.865
    JOURNAL FREE ACCESS
    Download PDF (614K)
  • A Vision of Zymophage
    Isamu OHKURO
    1984 Volume 39 Issue 6 Pages 869-871
    Published: November 25, 1984
    Released on J-STAGE: February 19, 2009
    DOIhttps://doi.org/10.3412/jsb.39.869
    JOURNAL FREE ACCESS
    Download PDF (499K)
  • A resistance mechanism to Cephem antibiotics in Staphylococcus aureus
    Reiko YOSHIDA
    1984 Volume 39 Issue 6 Pages 873-880
    Published: November 25, 1984
    Released on J-STAGE: February 19, 2009
    DOIhttps://doi.org/10.3412/jsb.39.873
    JOURNAL FREE ACCESS
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    The mechanism of the resistance to cephem-antibiotics was studied with two clinical isolates of Staphylococcus aureus, JS1 and JS2. Both strains were confirmed to produce β-lactamase possessing penicillinase-activity but no apparent cephalosporinase-activity. Non-β-lactamase-producing subclones, JS11 and JS21, obtained by curing the β-lactamase-encoding plasmid through cultivating JS1 and JS2 at 44C overnight, were as resistant to cephemantibiotics as the parent strains. This suggests that the resistance to cephem-antibiotics is not related to penicillinase.
    Fluorography of penicillin-binding proteins (PBPs) of JS11 and JS21 indicated that the intrinsically cephem-resistant strains possessed a specific 78 kilodalton (Kd) protein (PBP2') besides PBP1 (81Kd), PBP2 (77Kd), PBP3 (74Kd), and PBP4 (44Kd) proteins. The latter four PBPs were shown also in the respective sensitive strains, JS111 and JS211, obtained by 10 times successive subculturing of JS11 and JS21 in drug-free medium. The 78Kd protein hardly bound to 14C-penicillin G at a concentration of 0.01mM, Whereas the other PBPs, PBP1, PBP2, PBP3, and PBP4, in either the resistant parents or sensitive strains bound abundantly to it. A competitive binding study using non-radioactive cefoxitin and PCG revealed that less than 30% of the 78Kd protein (PBP2') was saturated with cefoxitin at a concentration of 25μg/ml, whereas 84% each of the other PBPs was saturated.
    Almost the same amounts of 14C-penicillin G bound to each of PBPs of the intrinsically resistant staphylococci with either the membrane fraction or whole live cells, indicating that no penetration barrier exists in the intrinsically cephem-resistant S. aureus.
    It was concluded that the two cephemresistant clinical isolates S. aureus possess a specific 78Kd PBP that catalyzes crosslinking of murein even in the presence of cephem-antibiotics because of its low affinity to the drugs.
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