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• W2003090198 abstract "Glutathione transport was studied in brush-border membrane vesicles of rabbit small intestine in which gamma-glutamyl transpeptidase (EC 2.3.2.2) had been inactivated by a specific affinity-labeling reagent, L-(alpha S,5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid (AT125). Transport of intact [glycine-2-3H]GSH occurred into an osmotically active intravesicular space of AT125-treated membranes. The 0.1 M NaSCN gradient (Na+ inside greater than Na+ outside) in the transport medium could be replaced with KSCN or NaCl without affecting transport activity. The initial rate of GSH transport followed Michaelis-Menten saturation kinetics (Km = 17 microM). The results suggest that, in these membranes, there was an Na+-independent mediated transport for intact GSH with marked specificity and affinity. In fact glycine, glutamic acid and cysteine did not decrease GSH uptake, as was also true for glycylglycine and glycylglycylglycine; only gamma-glutamylcysteinylglycyl ester, a derivative of GSH, partially inhibited GSH transport." @default.
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• W2003090198 date "1988-07-01" @default.
• W2003090198 modified "2023-10-18" @default.
• W2003090198 title "Glutathione-mediated transport across intestinal brush-border membranes" @default.
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• W2003090198 doi "https://doi.org/10.1016/0005-2736(88)90279-9" @default.
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