The Journal of General and Applied Microbiology
Online ISSN : 1349-8037
Print ISSN : 0022-1260
ISSN-L : 0022-1260
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Volume 27, Issue 4
Displaying 1-8 of 8 articles from this issue
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  • THE CELL CYCLE IN THE FISSION YEAST, SCHIZOSACCHAROMYCES POMBE. VI. RELATIONSHIP BETWEEN CELL SIZE AND DIVISION DELAY DUE TO NUTRITIONAL SHIFT-UP
    HISAO MIYATA, MACHIKO MIYATA, MICHIO ITO
    1981 Volume 27 Issue 4 Pages 277-285
    Published: 1981
    Released on J-STAGE: August 18, 2006
    DOIhttps://doi.org/10.2323/jgam.27.277
    JOURNAL FREE ACCESS
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    The shift of a synchronous culture of the fission yeast, Schizosaccharomyces pombe, from a poor to a rich medium resulted in division delay. The mean time period from the shift till division was nearly constant, regardless of the time of shift in the cell cycle.
    The time period from the shift till division of the individual cells was negatively proportional to cell size at the shift. The division size of the shifted cells was larger than that of exponentially proliferating cells. From these results, the dependence of the timing of division on cell size at the shift, not at division, is discussed.
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  • GROWTH RATE AND MOLAR GROWTH YIELD OF ESCHERICHIA COLI ADSORBED ON AN ANION-EXCHANGE RESIN
    REIKO HATTORI, TSUTOMU HATTORI
    1981 Volume 27 Issue 4 Pages 287-298
    Published: 1981
    Released on J-STAGE: August 18, 2006
    DOIhttps://doi.org/10.2323/jgam.27.287
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    Using a rapid continuous flow system (D=1), growth rates and molar growth yields of free and adsorbed cells of Escherichia coli were determined with glucose as a limiting substrate. In this system, free cells were continuously removed and a steady state in cell or substrate concentration in the liquid phase of culture was realized by the growth of adsorbed cells. Growth constants of free cells, μ and Y, were obtained from a washout curve of free cells and a corresponding curve of increase of a substrate. Growth constants of adsorbed cells, μa and Ya, were obtained from steady state concentrations of cell and substrate in the liquid phase of culture during cultivation of adsorbed cells.
    The growth rate of adsorbed cells depended both on substrate concentration and the amount of adsorbed cells. Saturation constants for growth, KS, with glucose as a substrate were extremely high and they also depended on the amount of adsorbed cells. The maximal growth rate and the molar growth yield of adsorbed cells were much higher than those of free cells.
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  • CHARACTERIZATION OF PLASMID DEOXYRIBONUCLEIC ACID IN BACILLUS NATTO: EVIDENCE FOR PLASMID-LINKED PGA PRODUCTION
    TOSHIO HARA, ANDREA AUMAYR, SEINOSUKE UEDA
    1981 Volume 27 Issue 4 Pages 299-305
    Published: 1981
    Released on J-STAGE: August 18, 2006
    DOIhttps://doi.org/10.2323/jgam.27.299
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    Treatment of Bacillus natto (Asahikawa) with acridine orange resulted in the conversion of approximately 64.2% of the population to stringiness negative, which is indicative of the involvement of plasmid deoxyribonucleic acid (DNA). Cleared lysate materials were subjected to agarose gel electrophoresis to determine the plasmid composition of each strain. B. natto (Asahikawa) was found to possess a plasmid of approximately 4.2 megadaltons (Mdal). A 4.2 Mdal plasmid has been found to be missing in the stringiness-negative mutants cured by acridine orange. Gamma-GTP activity was also deficient in the stg- mutants which were missing the 4.2 Mdal plasmid.
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  • ETUDE D'UNE L-α-AMINOAMIDASE PARTICULAIRE DE BREVIBACTERIUM SP. EN VUE DE L'OBTENTION D'ACIDES α-AMINES OPTIQUEMENT ACTIFS
    MARIE-PAULE KIENY-L'HOMME, ALAIN ARNAUD, PIERRE GALZY
    1981 Volume 27 Issue 4 Pages 307-325
    Published: 1981
    Released on J-STAGE: August 18, 2006
    DOIhttps://doi.org/10.2323/jgam.27.307
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    The L-α-aminoamidase of Brevibacterium A4 is a particle enzyme with a molecular weight of 135, 000; its optimum pH is 9.5 and its optimum temperature 60°. It is probably a metallo-enzyme with an SH group in the active site, and requiring the presence of Mg2+ or Mn2+. The purification tests showed that it hydrolyses a large number of α-aminoamides. The Michaelis constant Km varies little for the different substrates. On the other hand the Vm varies greatly, in particular according to the hydrocarbon chain length.
    The use of the α-amidoamidasic activity for the preparation of optically active, natural or non-natural α-aminoacids has been considered.
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  • TEMPERATURE-DEPENDENCE AND DISTRIBUTION OF NADH DEHYDROGENASE IN A PSYCHROPHILIC BACTERIUM, VIBRIO SP. STRAIN ABE-1
    YASUHIRO TAKADA, NORIYUKI FUKUNAGA, SHOJI SASAKI
    1981 Volume 27 Issue 4 Pages 327-337
    Published: 1981
    Released on J-STAGE: August 18, 2006
    DOIhttps://doi.org/10.2323/jgam.27.327
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    NADH dehydrogenase (EC 1.6.99.3), which catalyzes the first reaction of the NADH oxidase system known to operate actively at low temperature in Vibrio sp. strain ABE-1, was examined in respect of intracellular distribution, temperature- and salts-dependencies, and so on.
    Almost the same amount of the enzyme was distributed in the cytoplasmic and membrane fractions, and the enzymes in the two fractions were presumed to be different ones by virtue of their properties such as optimum pH, salts- and temperature-dependencies.
    Both enzymes were unique in that they were able to function at a remarkably high rate under lower temperatures: the activities at 5° were about 70% of the respective maximum activities.
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  • IMMOBILIZATION OF INVERTASE ON MOLECULAR SIEVE BY METAL-LINK METHOD
    LEELA IYENGAR, A. V. S. PRABHAKARA RAO
    1981 Volume 27 Issue 4 Pages 339-348
    Published: 1981
    Released on J-STAGE: August 18, 2006
    DOIhttps://doi.org/10.2323/jgam.27.339
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    Invertase is immobilized using an inorganic solid support, Molecular sieve 4A, via the metal link method. Bound enzyme showed maximum activity at pH 4.8 which was similar to that of soluble enzyme. Protein to solid support ratio was very critical for the retention of active invertase as loading beyond 18-20mg protein/g MS significantly decreased bound invertase activity. Km for the soluble and immobilized enzyme were found to be 20mM and 50mM respectively. Bound enzyme retained 90% original activity after 45 days at room temperature. Half-life for the continuous conversion of sucrose using MS-bound invertase was calculated to be 26 days. Used MS could be regenerated using perchloric acid. Regenerated MS did not require titanium activation and could retain 90% of the enzyme activity as compared to the control. Ammonium sulphate treatment was not effective in the regeneration of MS, indicating the enzyme is bound to MS by covalent linkage.
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  • REPRODUCTION BY MULTILATERAL BUDDING OF TWO STRAINS OF KLOECKERA CORTICIS
    SHOJI GOTO
    1981 Volume 27 Issue 4 Pages 349-351
    Published: 1981
    Released on J-STAGE: August 18, 2006
    DOIhttps://doi.org/10.2323/jgam.27.349
    JOURNAL FREE ACCESS
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  • CLOSE RELATIONSHIP BETWEEN BACILLUS PHAGES M2 AND Nf: PHYSICAL MAPPING OF THE DNA BY SIX RESTRICTION ENDONUCLEASES
    KOUJI MATSUMOTO, MICHIYO HIRUTA, YUKIKO MIZUKAMI, HIDEO HIROKAWA
    1981 Volume 27 Issue 4 Pages 353-356
    Published: 1981
    Released on J-STAGE: August 18, 2006
    DOIhttps://doi.org/10.2323/jgam.27.353
    JOURNAL FREE ACCESS
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