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  • Title: Biosynthesis in vitro of a sulfated triglucosyl monoalkylmonoacylglycerol by rat gastric mucosa.
    Author: Liau YH, Zdebska E, Slomiany A, Slomiany BL.
    Journal: J Biol Chem; 1982 Oct 25; 257(20):12019-23. PubMed ID: 6956577.
    Abstract:
    A sulfotransferase activity which catalyzes the transfer of the sulfate ester group from 3'-phosphoadenosine 5'-phosphosulfate to triglucosyl monoalkylmonoacylglycerol to form sulfated triglucosyl monoalkylmonoacylglycerol (SO3H-6Glc alpha 1 leads to 6Glc alpha 1 leads to 6Glc alpha 1 leads to 3-1,(3)-O-alkyl-2-O-acylglycerol) has been demonstrated in the rat gastric mucosa. The most enzyme activity was found in the cytosol fraction. Optimum enzymatic activity was obtained using the detergent Triton X-100, F1-, and Mg2+ at a pH of 7.8. The ATP, ADP, and dithiothreitol had inhibitory effects on the sulfotransferase. The enzymatic activity increased proportionally, over a given range, with increased concentrations of both substrates and of enzyme. The apparent Km of the enzyme for triglucosyl monoalkylmonoacylglycerol was 6.9 x 10(-5) M, and for 3'-phosphoadenosine 5'-phosphosulfate, 8.5 x 10(-7) M. The enzyme did not catalyze the transfer of sulfate to galactosylceramide. The results of compositional analyses and permethylation studies of the 35S-labeled product of the enzymatic reaction established that the sulfate ester group is located at C-6 on the terminal glucose residue.
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