pH-dependent heterogeneity of acidic amino acid transport in rabbit jejunal brush border membrane vesicles

Initial rates of Na(+)-dependent L-glutamic and D-aspartic acid uptake were determined at various substrate concentrations using a fast sampling, rapid filtration apparatus, and the resulting data were analyzed by nonlinear computer fitting to various transport models. At pH 6.0, L-glutamic acid tra...

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Bibliographic Details
Published inThe Journal of biological chemistry Vol. 267; no. 3; pp. 1510 - 1516
Main Authors Maenz, D D, Chenu, C, Breton, S, Berteloot, A
Format Journal Article
LanguageEnglish
Published Bethesda, MD Elsevier Inc 25.01.1992
American Society for Biochemistry and Molecular Biology
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Summary:Initial rates of Na(+)-dependent L-glutamic and D-aspartic acid uptake were determined at various substrate concentrations using a fast sampling, rapid filtration apparatus, and the resulting data were analyzed by nonlinear computer fitting to various transport models. At pH 6.0, L-glutamic acid transport was best accounted for by the presence of both high (Km = 61 microM) and low (Km = 7.0 mM) affinity pathways, whereas D-aspartic acid transport was restricted to a single high affinity route (Km = 80 microM). Excess D-aspartic acid and L-phenylalanine served to isolate L-glutamic acid flux through the remaining low and high affinity systems, respectively. Inhibition studies of other amino acids and analogs allowed us to identify the high affinity pathway as the X-AG system and the low affinity one as the intestinal NBB system. The pH dependences of the high and low affinity pathways of L-glutamic acid transport also allowed us to establish some relationship between the NBB and the more classical ASC system. Finally, these studies also revealed a heterotropic activation of the intestinal X-AG transport system by all neutral amino acids but glycine through an apparent activation of Vmax.
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ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)45975-3