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: Gamma-glutamyl transpeptidase-mediated transport of amino acid in lecithin vesicles.
    Author: Sikka SC, Kalra VK.
    Journal: J Biol Chem; 1980 May 25; 255(10):4399-402. PubMed ID: 6102987.
    Abstract:
    Gamma-Glutamyl transpeptidase, a membrane-bound enzyme purified from hog kidney cortex following solubilization with detergent, was incorporated by sonication procedure into large phospholipid vesicles using a 1:2 molar ratio of deoxycholate to phospholipid. tthese vesicles, when containing entrapped glutathione, exhibited the uptake of L-[14C]glutamate, but not of L-proline. The glutamate uptake did not occur to a significant extent in these vesicles when glutathione was added externally. The uptake of glutamate in the reconstituted system was sensitive to the temperature of incubation and to the inhibitors (serine-borate, azaserine, and 6-diazo-5-oxo-L-norleucine) of gamma-glutamyl transpeptidase activity. The accumulated product during the transport of glutamate in the gamma-glutamyl transpeptidase reconstituted system containing intravesicular glutathione was identified as gamma-glutamyl-glutamate. These results indicate that gamma-glutamyl transpeptidase mediates the translocation of glutamate in vitro and provides evidence in support of its role in the transport of amino acids in natural membranes.
    [Abstract] [Full Text] [Related] [New Search]