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  • 1
    Electronic Resource
    Electronic Resource
    Purification and partial characterization of ad(−)-lactate dehydrogenase fromDesulfovibrio desulfuricans (ATCC 7757) (1990)
    Springer
    Journal of industrial microbiology and biotechnology 6 (1990), S. 117-122 
    Details
    ISSN: 1476-5535
    Keywords: d(−)-Lactate dehydrogenase ; Membrane-bound protein ; Sulfate-reducing bacterium ; Desulfovibrio desulfuricans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A membrane-boundd(−)-lactate dehydrogenase (LDH), an important enzyme in carbon and energy metabolism in sulfate-reducing bacteria of the genusDesulfovibrio, was solubilized from the membrane fraction ofDesulfovibrio desulfuricans (ATCC 7757). The enzyme was purified 84-fold to a final specific activity of 525 nmol DCPIP-reduced/min/mg protein by ammonium sulfate precipitation, chloroform extraction, gel filtration with Sephadex G-150, and hydrophobic column chromatography withN-octylamine Sepharose 4B. The enzyme eluted off a Sephacryl S-300 column as a single peak with a molecular weight of 400 000±40 000 Da. Denaturing gel electrophoresis showed it to be composed of 5 protein bands. The oxidized and dithionite reduced spectra of LDH resembles the spectra ofc-type cytochromes found inDesulfovibrio species. The addition of lactate to LDH resulted in a partially reduced spectrum. The flavin/cytochromec/non-heme iron content per 400 000 Da LDH molecular weight was found to be 1∶1.6∶4.5. The LDH activity was specific ford(−)-lactate and had aK m ford(−)-lactate of 4.3×10−4 M. The pH optimum was between 6.5 and 8.5.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01576430
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Utilization of cathodically-produced hydrogen from mild steel byDesulfovibrio species with different types of hydrogenases (1990)
    Springer
    Journal of industrial microbiology and biotechnology 6 (1990), S. 227-233 
    Details
    ISSN: 1476-5535
    Keywords: Desulfovibrio ; Hydrogenase ; Corrosion ; Iron ; FeS ; Hydrogen, cathodically produced
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Desulfovibrio (D.) vulgaris Hildenborough with a highly active Fe-containing periplasmic hydrogenase,D. salexigens British Guiana with a Fe−Ni−Se periplasmic hydrogenase, andD. multispirans with a Fe−Ni cytoplasmic hydrogenase utilized cathodically-produced hydrogen from mild steel as the only energy source for activity and growth. Changes on the mild steel surface occurred during growth of these bacteria. The concentration of iron sulfide, a corrosion product of mild steel, increased over time, andDesulfovibrio species had an active hydrogenase when they were grown in lactate/sulfate media. This hydrogenase may be any of the three types found in the genus,Desulfovibrio. The concentration of iron in the media affected the production and activity of the Fe-hydrogenase fromD. vulgaris Hildenborough. With an iron-limited medium, the specific activity and the total amount of the periplasmic hydrogenase was less than found with a non-iron limited media.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01575866
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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