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  • Bacillus sp.  (1)
  • Hordeum  (1)
  • Springer  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Analysis and in situ hybridization of cryptic satellites in Hordeum arizonicum (1986)
    Springer
    Theoretical and applied genetics 73 (1986), S. 40-46 
    Details
    ISSN: 1432-2242
    Keywords: DNA characterization ; Cryptic satellites ; Cytological localization ; Buoyant density ; Thermal denaturation ; Hordeum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Three satellites, one (H1) on the heavy side of the main band of Hordeum arizonicum DNA and two (L1, L2) on the lighter side were purified using preparative silver-cesium sulphate density gradients. The native and the reassociated satellite DNAs were analysed in terms of buoyant densities and thermal dissociation. In cesium chloride gradients the H1 and L1 satellites formed single peaks corresponding to buoyant densities of 1.700 and 1.701 g · cm−3 respectively while the L2 satellite gave two peaks (1.680 and 1.661 g · cm−3). The H1 satellite showed three thermal components (Tm=82.5 °C, 87 °C and 91.5 °C) while the L1 and L2 had three (86.5, 92, 97.5 °C) and two (86, 95 °C) respectively. The H1 satellite was localized on the nuclei and chromosomes. The distribution of H1 onto approximately on third of the complement may reflect the genome specific origin of this satellite.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00273716
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  • 2
    Electronic Resource
    Electronic Resource
    Short communication: Thermostability of α-amylase produced by Bacillus sp. E2—a thermophilic mutant (1995)
    Springer
    World journal of microbiology and biotechnology 11 (1995), S. 593-594 
    Details
    ISSN: 1573-0972
    Keywords: α-Amylase ; Bacillus sp. ; thermostability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract An α-amylase from a hyper-producing strain of Bacillus (sp. E2) was stable at 70°C for 30 min but was quickly inactivated at higher temperatures. In the presence of 10mm Ca2+ and starch (20% w/v), however, the enzyme was stable at 90°C for 10 min and after 30 min at 100°C still retained 26% of its initial activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00286380
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