These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Effect of ethanol on the enzymatic sulfation of glycosphingolipids in gastric mucosa.
    Author: Slomiany A, Jozwiak Z, Liau YH, Murty VL, Slomiany BL.
    Journal: J Biol Chem; 1984 May 10; 259(9):5792-6. PubMed ID: 6585364.
    Abstract:
    The enzyme activity which catalyzes the transfer of sulfate group from 3'-phosphoadenosine 5'-phosphosulfate to C-3 of the galactose residue of galactosylceramide and lactosylceramide has been demonstrated in the Triton X-100 extracts of the microsomal fraction of rat gastric mucosa. The sulfotransferase activity of this fraction in antral mucosa was 1.2-1.3 times greater than that of the body and 19-22 times greater than that of the forestomach. The enzyme did not catalyze the transfer of sulfate to glucosylceramide, trihexosylceramide, and triglucosyl monoalkylmonoacylglycerol. Optimum enzymatic activity was obtained using 0.4% Triton X-100, 33 mM NaF, and 15 mM MgCl2 at a pH of 6.8. The sulfotransferase activity was inhibited by ethanol. With both glycolipid substrates, little inhibition of enzyme activity was obtained up to 0.5 M ethanol. However, higher concentrations of ethanol produced severe inhibitory effect. This inhibition of sulfation of galactosylceramide and lactosylceramide by ethanol was of the competitive type. The apparent KI values were 8.3 X 10(-5) for galactosylceramide and 5.6 X 10(-5) for lactosylceramide.
    [Abstract] [Full Text] [Related] [New Search]