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  • enzyme kinetics  (2)
  • Springer  (2)
  • American Chemical Society (ACS)
  • 1
    Electronic Resource
    Electronic Resource
    A transmembranous NADH-dehydrogenase in human erythrocyte membranes (1984)
    Springer
    Journal of bioenergetics and biomembranes 16 (1984), S. 517-533 
    Details
    ISSN: 1573-6881
    Keywords: Transmembranous NADH-dehydrogenase ; enzyme kinetics ; human erythrocyte ; plasma membrane
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Evidence is presented for a transmembranous NADH-dehydrogenase in human erythrocyte plasma membrane. We suggest that this enzyme is responsible for the ferricyanide reduction by intact cells. This NADH-dehydrogenase is distinctly different from the NADH-cytochromeb 5 reductase on the cytoplasmic side of the membrane. Pretreatment of erythrocytes with the nonpenetrating inhibitor diazobenzene sulfonate (DABS) results in a 35% loss of NADH-ferricyanide reductase activity in the isolated plasma membrane. Since NADH and ferricyanide are both impermeable, the transmembrane enzyme can only be assayed in open membrane sheets with both surfaces exposed, and not in closed vesicles. The transmembrane dehydrogenase has affinity constants of 90 µM for NADH and 125 µM for ferricyanide. It is inhibited byp-chloromercuribenzoate, bathophenanthroline sulfonate, and chlorpromazine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00743243
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  • 2
    Electronic Resource
    Electronic Resource
    Transplasmalemma electron transport is changed in simian virus 40 transformed liver cells (1986)
    Springer
    Journal of bioenergetics and biomembranes 18 (1986), S. 471-485 
    Details
    ISSN: 1573-6881
    Keywords: Plasma membrane ; pyridine nucleotide oxidation ; temperature sensitive SV40 ; liver cells ; transmembrane electron transport ; cell transformation ; enzyme kinetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Transplasma membrane electron transport activity by fetal rat liver cells (RLA209-15) infected with a temperature-sensitive strain of SV40 has been measured with cells grown at the restrictive temperature (40°C) and permissive temperature (33°C). The transformed cells grown at 33°C had only one-half the rate of external ferricyanide reduction as the nontransformed cells held at 40°C. Both theK m andV max for ferricyanide reduction were changed in the transformed state. The change inV max can be based on a decrease of NADH in the transformed cells. The change in rate with ferricyanide does not depend on change in surface charge. Reduction of external ferricyanide was accompanied by release of protons from the cells. The ratio of protons released to ferricyanide reduced was higher in the transformed cells than in the non-transformed cells. Since the transplasma membrane electron transport has been shown to stimulate cell growth under limiting serum, the changes in the plasma membrane electron transport and proton release in transformed cells may relate to modification of growth control.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00743145
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