ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • Articles  (3)
  • Glycine decarboxylase  (2)
  • Acetogenium kivui  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 129 (1981), S. 275-280 
    ISSN: 1432-072X
    Keywords: Acetogenium kivui ; Thermophilic acetogenic bacteria ; Hydrogen oxidation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Hydrogen-oxidizing acetogenic bacteria in pure culture are presently represented by the two mesophilic species, Acetobacterium woodii and Clostridium aceticum. From Lake Kivu we have isolated a Gram negative, chemolithotrophic, thermophilic anaerobe (LKT-1) that oxidizes hydrogen and reduces carbon dioxide to acetic acid. It is a non-motile, non-sporeforming rod, about 0.7μm in width and 2–7.5μm in length, often occuring in pairs or chains. The cell wall has a banded appearance; the surface layer contains a regular array of particles with six-fold rotational symmetry. No outer membrane is present. The temperature optimum for growth is 66°C, and the pH optimum is 6.4. Organic growth substrates include glucose, mannose, fructose, pyruvate, and formate; acetate is the principal product. The doubling time for growth on hydrogen and carbon dioxide is about 2h. Vitamins are neither required nor stimulatory. Yeast extract and Trypticase enhance the final yield but do not affect the growth rate. Cysteine or sulfide are required and cannot be replaced by thioglycolate or dithiothreitol. LKT-1 was mass cultured on hydrogen and carbon dioxide in a 24.1 fermentor with a yield of 34g (wet weight) of cells. The DNA base composition as determined by buoyant density is 38 mol % guanine plus cytosine. LKT-1 appears only distantly related to physiologically similar bacteria. A new genus Acetogenium is proposed, and the species is Acetogenium kivui.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1432-072X
    Keywords: Clostridium cylindrosporum ; Dihydrolipoamide dehydrogenase ; Glycine decarboxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Immunocytochemical localization experiments were performed with antibodies raised against the dihydrolipoamide dehydrogenase protein (P3) of the glycine decarboxylase complex from clostridium cylindrosporum using the low-temperature procedure and protein A-gold technique. An association with the cytoplasmic membrane was indicated to about 65 (±10) % when cells were analyzed from the logarithmic growth phase. The unusual peripheral localization is discussed.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 1432-072X
    Keywords: Glycine decarboxylase ; Glycine reductase ; Lipoamide dehydrogenase ; Selenoprotein PA ; Eubacterium acidaminophilum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Antibodies raised against the glycine decarboxylase proteins P1, P2, P3, and the selenoprotein PA, a component of the glycine reductase complex, were used for immunocytochemical localization experiments. Cells of Eubacterium acidaminophilum from logarithmic growth phase were fixed in the growth media with paraformaldehyde and glutaraldehyde. Fixed cells were embedded by the low-temperature procedure using Lowicryl K4M resin, and the protein A-gold technique was applied for the localization experiments. The vicinity of the cytoplasmic membrane contained about 27% of all gold particles when proteins P1 and P2 were to be localized, 50% for protein PA, and 61% for protein P3. Double immunocytochemical labeling experiments gave evidence for the existence of a protein P1/P2 complex located predominantly in the cytoplasm, and a P3/PA complex located at the cytoplasmic membrane. Only in very few instances the labels for proteins P3 and P1 were seen very close together in respective doublelabeling experiments. These results indicate that glycine decarboxylase does not occur in this organism as a complex consisting of all four proteins, but that protein P3, the atypical lipoamide dehydrogenase, takes part in both the glycine decarboxylase as well as in the glycine reductase reaction.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...