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  • Title: Chemical properties of the anion transport inhibitory binding site of arginine-specific reagents in human red blood cell membranes.
    Author: Julien T, Betakis E, Zaki L.
    Journal: Biochim Biophys Acta; 1990 Jul 09; 1026(1):43-50. PubMed ID: 2378880.
    Abstract:
    A series of arginine-specific reagents with different size and polarity have been synthesized and their inhibitory potency on sulfate exchange in resealed ghosts has been investigated. The synthesized phenylglyoxal derivatives p-nitro-, p-methyl-, p-hydroxy-, p-carboxy-, p-sulfo-, and p-azido-phenylglyoxal are found to be potent inhibitors of anion transport. The reaction between the cells and azidophenylglyoxal was performed in the dark. Exposure of the modified cells to the light was not followed by an increase in the inhibition. No cross-linking products were visible after gel electrophoresis. The rate of inactivation of sulfate flux with these reagents obeyed pseudo-first-order kinetics and increases with increasing reagents concentration and pH. Prolonged incubation of the cells with these reagents results in almost complete inhibition of the transport system. The positively charged phenylglyoxal derivative 4-(trimethylammonioacetylamido)phenylglyoxal was not able to inhibit the transport system. The hydrophobic character and the electronic properties of these reagents do not correlate with their inhibitory potency. Their electrostatic and steric effects seem to play the major role in their action.
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