Nippon Saikingaku Zasshi
Online ISSN : 1882-4110
Print ISSN : 0021-4930
ISSN-L : 0021-4930
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Volume 30, Issue 2
Displaying 1-9 of 9 articles from this issue
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  • Genetics in Mycrobacteria
    Yasuo MIZUGUCHI, Tohru TOKUNAGA
    1975 Volume 30 Issue 2 Pages 297-313
    Published: March 25, 1975
    Released on J-STAGE: February 19, 2009
    DOIhttps://doi.org/10.3412/jsb.30.297
    JOURNAL FREE ACCESS
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  • Mutation of a Clostridium perfringens Type D Strain Treated with Acriflavine
    Fusao KONDO, Manabu OGATA
    1975 Volume 30 Issue 2 Pages 315-325
    Published: March 25, 1975
    Released on J-STAGE: February 19, 2009
    DOIhttps://doi.org/10.3412/jsb.30.315
    JOURNAL FREE ACCESS
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    Acriflavine-treated substrains of the Clostridium perfringens type D strain Lam 61 were examined for colonial morphology, biochemical properties, toxigenicity, sporulation, and antigenic properties. On the basis of the difference in the colonial morphology on Zeissler's plate, 10 substrains were established. Of these mutants, seven were ε-toxigenic and the remaining three non-toxigenic. Further studies revealed that the rougher the colonies of these mutants, the great the length of the cells, and that some of these mutants were deficient in ability to ferment several sugars, had an attenuated ability to sporulate, and were more agglutinable spontaneously than the parent strain.
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  • Comparison of Amino Acid Composition, Immunological Properties, and Molecular Weight of Fimbriae of Gram-Nagative Bacteria
    Sankichi HORIUCHI
    1975 Volume 30 Issue 2 Pages 327-338
    Published: March 25, 1975
    Released on J-STAGE: February 19, 2009
    DOIhttps://doi.org/10.3412/jsb.30.327
    JOURNAL FREE ACCESS
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    The fimbriae of the genera Shigella, Escherichia, Klebsiella, Aeromonas, and Serratia were purified. Their purities were proved by electron microscopy, immunodiffusion, and SDS polyacrylamide gel electrophoresis. The purified fimbriae were used to determine the molecular weight of the fimbrial subunits, and the amino acid composition and immunological properties of the fimbriae.
    The mannose-sensitive (MS-type) fimbriae of Shigella flexneri, Escherichia coli, and Klebsiella pneumoniae had some similarities in amino acid composition, containing more alanine, aspartic acid, and threonine. In them, neutral and acidic amino acids were abundant, but the molar percentage of basic amino acids ranged from 3 to 5. The fimbriae of Aeromonas hydrophila contained more glycine, alanine, and glutamic acid than those of any other organism. In contrast, the mannose-resistant type fimbriae of Serratia marcescens contained more lysine, which is a basic amino acid, aspartic acid, and alanine than those of any other organism. The molar percentage of basic amino acids was about 24. These results indicated that there was a marked difference in the characters of the fimbriae between Serratia and any others species.
    The MS-type fimbriae of the 3 species also shared remarkable similarity in immunologicall properties, but those of the other 2 species differed a little from each other.
    The molecular weights of the subunits of the fimbriae of all the bacterial species studied were estimated to be about 17, 000 by SDS polyacrylamide gel electrophoresis.
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  • Studies on the Bacterial Spore Cortex
    I. Comparison of Peptidoglycan Between the Spore and Vegetative Cell of Bacillus subtilis NRRL B558
    Keiji SANO, Tomio ICHIKAWA, Masaomi KONDO
    1975 Volume 30 Issue 2 Pages 339-345
    Published: March 25, 1975
    Released on J-STAGE: February 19, 2009
    DOIhttps://doi.org/10.3412/jsb.30.339
    JOURNAL FREE ACCESS
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    The chemical structure was compared between peptidoglycan from the spore of Bacillus subtilis NRRL B558 and that from the vegetative cell. Thirty to forty percent of the muramic acid residues of the spore peptidoglycan was found to be substituted by no peptides. The other portion of the residues was substituted mostly by L-alanyl-D-glutamyl-diaminopimelyl-D-alanine or L-alanine. A small amount of cross-linked peptide was also found in the spore peptidoglycan. On the other hand, the muramic acid residues of the vegetative-cell peptidoglycan were fully substituted by cross-linked peptide.
    These results suggest that the chemical structure of the spore peptidoglycan may not be so solid as that of the vegetative-cell peptidoglycan.
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  • Rapid Measurement of Heat Resistance of Bacillus cereus T spores
    Isamu TANI, Tomoko SAGARA, Hirofumi SHIBATA
    1975 Volume 30 Issue 2 Pages 347-348
    Published: March 25, 1975
    Released on J-STAGE: February 19, 2009
    DOIhttps://doi.org/10.3412/jsb.30.347
    JOURNAL FREE ACCESS
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  • [title in Japanese]
    1975 Volume 30 Issue 2 Pages 349-379
    Published: March 25, 1975
    Released on J-STAGE: February 19, 2009
    DOIhttps://doi.org/10.3412/jsb.30.349
    JOURNAL FREE ACCESS
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  • [title in Japanese]
    1975 Volume 30 Issue 2 Pages 380-386
    Published: March 25, 1975
    Released on J-STAGE: February 19, 2009
    DOIhttps://doi.org/10.3412/jsb.30.380
    JOURNAL FREE ACCESS
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  • [title in Japanese]
    1975 Volume 30 Issue 2 Pages 387-396
    Published: March 25, 1975
    Released on J-STAGE: February 19, 2009
    DOIhttps://doi.org/10.3412/jsb.30.387
    JOURNAL FREE ACCESS
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  • [title in Japanese]
    1975 Volume 30 Issue 2 Pages 397-410
    Published: March 25, 1975
    Released on J-STAGE: February 19, 2009
    DOIhttps://doi.org/10.3412/jsb.30.397
    JOURNAL FREE ACCESS
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