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  • 1985-1989  (2)
  • 1965-1969
  • Blue light  (1)
  • Klebsiella pneumoniae  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Action spectrum for the blue-light-dependent morphogenesis of hair whorls in Acetabularia mediterranea (1987)
    Springer
    Planta 171 (1987), S. 96-103 
    Details
    ISSN: 1432-2048
    Keywords: Acetabularia ; Action spectrum ; Blue light ; Hair whorls (Acetabularia) ; Photomorphogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In young Acetabularia mediterranea Lamouroux (=A. acetabulum (L.) Silva) the formation of the lateral hair whorls can be induced by a short pulse of blue light after continuous red preillumination. In this paper we describe the experimental conditions for optimum response and the properties of the action spectrum. The probit of the cells which eventually form hair whorls is linearly correlated to the logarithm of the incident quanta of blue light. Parallel fluence-response curves for all wavelengths indicate the involvement of only one photoreceptor pigment. The action spectrum shows no effectiveness of wavelengths above 520 nm, a high action peak at 470 nm and two lower ones at 425 and 370 nm, and is in accordance with those of cryptochrome-like photoreceptors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00395072
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Evolutionary relationship between Enterobacteriaceae: comparison of the ATP synthases (F1F0) of Escherichia coli and Klebsiella pneumoniae (1987)
    Springer
    Archives of microbiology 148 (1987), S. 187-192 
    Details
    ISSN: 1432-072X
    Keywords: F1F0 ATP synthase ; Escherichia coli ; Klebsiella pneumoniae ; Phylogenetic relationship
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The ATP synthase complex of Klebsiella pneumoniae (KF1F0) has been purified and characterized. SDS-gel electrophoresis of the purified F1F0 complexes revealed an identical subunit pattern for E. coli (EF1F0) and K. pneumoniae. Antibodies raised against EF1 complex and purified EF0 subunits recognized the corresponding polypeptides of EF1F0 and KF1F0 in immunoblot analysis. Protease digestion of the individual subunits generated an identical cleavage pattern for subunits α, β, γ, ε, a, and c of both enzymes. Only for subunit δ different cleavage products were obtained. The isolated subunit c of both organisms showed only a slight deviation in the amino acid composition. These data suggest that extensive homologies exist in primary and secondary structure of both ATP synthase complexes reflecting a close phylogenetic relationship between the two enterobacteric tribes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414810
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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