Nippon Saikingaku Zasshi
Online ISSN : 1882-4110
Print ISSN : 0021-4930
ISSN-L : 0021-4930
Volume 40, Issue 2
Displaying 1-6 of 6 articles from this issue
  • Ichiro TAKAZOE
    1985 Volume 40 Issue 2 Pages 459-470
    Published: March 25, 1985
    Released on J-STAGE: February 19, 2009
    JOURNAL FREE ACCESS
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  • From phage research to animal virus research
    Hisao UETAKE
    1985 Volume 40 Issue 2 Pages 471-476
    Published: March 25, 1985
    Released on J-STAGE: February 19, 2009
    JOURNAL FREE ACCESS
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  • Hiroko USAMI
    1985 Volume 40 Issue 2 Pages 477-499
    Published: March 25, 1985
    Released on J-STAGE: February 19, 2009
    JOURNAL FREE ACCESS
    1. The M protein of Streptococcus pyogenes (type 3, strain Sv) was solubilized by treatment of a cell envelope fraction with endo-N-acetylmuramidase (the M-1 enzyme). It was concentrated by salting out at 30-80% saturation of ammonium sulfate and fractionated on a QAE-Sephadex column by elution with a linear gradient of sodium chloride concentration.
    2. The M protein thus isolated (mur M3) was shown to be practically a homogeneous protein with a molecular weight of 150, 000-160, 000 daltones and an isoelectric point of 5.9 in SDS-polyacrylamide gradient gel electrophoresis (PAGE) and PAGE, respectively, and to give essentially a single precipitin line with anti-Sv whole cell rabbit serum and anti-mur M3 guinea-pig serum in Ouchterlony's agar gel precipitin reaction.
    3. Mur M3 composed almost exclusively of amino acids, contained neither muramic acid nor glucosamine, but contained trace amounts of rhamnose and organic phosphorus.
    4. Mur M3 exhibited a distinct type-specific, opsonin-neutralizing activity which was susceptible to trypsin but resistant to boiling in 0.2N HCl.
    5. Mur M3 was mitogenic on murine thymocytes, but not on murine splenocyte, and activated the human complement system via the classical as well as an alternate pathway.
    6. Mur M3 was immunogenic to guinea pigs, rabbits and mice, especially to guinea pigs. Two intra-footpad injections of 10μg amounts of mur M3 into guinea pigs without any adjuvant stimulated a distinct and long-lasting production of anti-M3 opsonizing and protective antibody.
    The results described in this report suggest that mur M3 is a more native M protein than those so far obtained by other researchers.
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  • Shinichi NARIKAWA, Isao HARASAWA, Masao NAKAMURA
    1985 Volume 40 Issue 2 Pages 501-509
    Published: March 25, 1985
    Released on J-STAGE: February 19, 2009
    JOURNAL FREE ACCESS
    Streptococcus faecalis cells were sonically treated, and the extract of the treated cells was filtered through a 0.45-μm filter to remove the living organism. The cell-free extract was assayed for metronidazole-inactivating and nitroreductase activities, the latter being regarded as the inactivating factor.
    Metronidazole, a nitroimidazole derivative, was rapidly inactivated in broth by the cell-free extract of S. faecalis as measured by GLC and bioassay. As the rate of inactivation varied depending upon the medium and as the inactivating activity of the cell-free filtrate was not detected in broth cultures of the organism, the activity may occasionally be overlooked. The inactivating factor was produced in either the absence or the presence of oxygen and not induced by metronidazole but a constituent factor.
    The metronidazole-inactivating activity was detected also in cell-free extracts of Escherichia coli but not of Streptococcus agalactiae, Staphylococcus aureus or Serratia marcescens as was the case with the living organisms.
    Nitroreductase activity was detected in the cell-free extracts of the microbes inactivating metronidazole, but not of those not inactivating the drug.
    It is assumed that metronidazole is inactivated when its nitro-group is reduced by the action of nitroreductase in the cell-free extract of S. faecalis.
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  • 1985 Volume 40 Issue 2 Pages 511-526
    Published: March 25, 1985
    Released on J-STAGE: February 19, 2009
    JOURNAL FREE ACCESS
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  • 1985 Volume 40 Issue 2 Pages 527-543
    Published: March 25, 1985
    Released on J-STAGE: February 19, 2009
    JOURNAL FREE ACCESS
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