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  • Alcohol dehydrogenase  (1)
  • Defective prophages  (1)
  • Flagellation  (1)
  • 2020-2022
  • 1975-1979  (3)
  • 1935-1939
  • 1
    Electronic Resource
    Electronic Resource
    Micromorphology of Gram-negative hydrogen bacteria (1977)
    Springer
    Archives of microbiology 114 (1977), S. 93-100 
    Details
    ISSN: 1432-072X
    Keywords: Ultrastructure ; Micromorphology ; Gram-negative hydrogen bacteria ; Flagellation ; Flagellar fine structure ; Pili
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cell morphology, the arrangement and fine structure of flagella and the piliation of the following Gram-negative aerobic hydrogen bacteria have been studied: Alcaligenes eutrophus, Alcaligenes paradoxus, Alcaligenes ruhlandii, Pseudomonas flava, Pseudomonas pseudoflava, Pseudomonas palleronii, Pseudomonas facilis, Aquaspirillum autotrophicum, Paracoccus denitrificans, Corynebacterium autotrophicum, and strains MA 2 and SA 35. The identity of the bacteria was examined by their substrate spectra and type of flagellation. Three types of flagellar fine structure were differentiated. The presence of pili was noted in strains of Alcaligenes paradoxus, Pseudomonas flava, P. pseudoflava, P. palleronii, and P. facilis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00410769
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  • 2
    Electronic Resource
    Electronic Resource
    Electron microscopic study on the quaternary structure of the isolated particulate alcohol-acetaldehyde dehydrogenase complex and on its identity with the polygonal bodies of Clostridium kluyveri (1979)
    Springer
    Archives of microbiology 120 (1979), S. 255-262 
    Details
    ISSN: 1432-072X
    Keywords: Alcohol dehydrogenase ; Acetaldehyde dehydrogenase ; Clostridium kluyveri ; Electron microscopy ; Polygonal bodies ; Enzyme complex
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The alcohol-acetaldehyde dehydrogenase complex of Clostridium kluyveri has been separated from contaminating β-hydroxybutyryl-CoA dehydrogenase by repeated precipitation with manganese and ammonium sulfate. Mn++ was required for maximum alcohol dehydrogenase activity. The molecular weight of the enzyme complex was 194,000 as determined by sucrose density gradient centrifugation. The enzyme complex has been shown to contain two types of subunits with molecular weights of 55,000±2,600 and 42,000±1,200, respectively which are arranged in “H”-shaped particles. In solutions with an ionic strength above 25 mM the enzyme complex precipitated in the form of lumps as has been shown with specific ferritin-conjugated antibodies. These lumps are assumed to be aggregated polygonal bodies present in C. kluyveri.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00423073
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  • 3
    Electronic Resource
    Electronic Resource
    R-Bodies in newly isolated free-living hydrogen-oxidizing bacteria (1979)
    Springer
    Archives of microbiology 121 (1979), S. 9-15 
    Details
    ISSN: 1432-072X
    Keywords: R-Bodies ; Kappa particles ; Free-living hydrogen bacteria ; Induction ; Electron microscopy ; Chemical composition ; Defective prophages ; Plasmids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract R-Bodies have been found in a recently isolated pseudomonas-like free-living hydrogen oxidizing bacterium. Their isolation, fine structure and chemical composition are described and compared with the R-bodies from the kappa particles (Caedobacter), obligate endosymbionts of Paramecium aurelia. The 2K 1 R-bodies exhibited essential characteristics of the kappa R-bodies; however, their size and some other structural aspects proved that they represent a new type of R-bodies. The presence of phage tail-like particles in cells induced with Mitomycin C is in favour of the hypothesis that the R-bodies might be coded by defective prophages, or by extrachromosomal elements.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409199
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