Low-affinity intestinal L-aspartate transport with 2:1 coupling stoichiometry for Na+/Asp.
Low-affinity intestinal L-aspartate transport with 2:1 coupling stoichiometry for Na+/Asp.
复制标题
Na /Asp 的低亲和力肠道 L-天冬氨酸转运采用 2:1 耦合化学计量。
DOI:
10.1152/ajpcell.1988.255.6.c737
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发表时间:
1988
期刊:
影响因子:
--
通讯作者:
Kimmich,GA
中科院分区:
文献类型:
--
作者:
Wingrove,TG;Kimmich,GA
Epithelial cells isolated from chick small intestine were used to define the ionic and electrical characteristics of a low-affinity (Km = 4.1 mM) L-aspartate transport system. L-Glutamate and D-aspartate, but not D-glutamate, were found to inhibit L-aspartate influx, suggesting that this uptake system has a substrate specificity similar to that previously described for a high-affinity (Km = 16 microM) acidic amino acid transporter in the same cells. Low-affinity uptake is Na+ dependent with a Hill coefficient (n) of 1.4. Intracellular K+ moderately enhances but is not required for aspartate influx, and this response is modulated by changes in intracellular pH. The Na+-dependent uptake of aspartate is electroneutral, as evidenced by insensitivity to pronounced changes in delta psi induced by anion gradients or valinomycin in the presence of K+ gradients. Because the above characteristics can be consistent with several transport models, direct measurement of delta Na+-delta Asp coupling stoichiometry were performed. The coupling ratio was determined to be approximately 2.0. A model for intestinal Na+-dependent L-Asp transport is suggested in which each transport cycle involves inward transfer of 2Na+:1Asp+ and outward transfer of K+ or H+ in a net electroneutral set of events.