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Amino acid transport in brush-border-membrane vesicles isolated from human small intestine

MPG-Autoren
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Lücke,  Heinrich
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Haase,  Winfried
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Murer,  Heini
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Zitation

Lücke, H., Haase, W., & Murer, H. (1977). Amino acid transport in brush-border-membrane vesicles isolated from human small intestine. Biochemical Journal, 168(3), 529-532. doi:10.1042/bj1680529.


Zitierlink: https://hdl.handle.net/21.11116/0000-0008-6E11-A
Zusammenfassung
Uptake of L-alanine and L-phenylalanine by purified bursh-border-membrane vesicles isolated from human small intestine was investigated by using a rapid-filtration technique. L-Alanine entered the same osmotically reactive space as D-glucose, indicating that transport into the vesicle rather than binding to the membranes was being observed. The uptake rate for L-alanine was higher in the presence of a Na+ gradient than in the presence of a K+ gradient. In the presence of a Na+ gradient, the lipophilic anion SCN+ caused an increase in L-alanine transport, whereas the nearly impermeant SO42- anion decreased the uptake of L-alanine compared with its uptake in the presence of Cl-. The uptake of L-phenylalanine into the brush-border-membrane vesicle was also stimulated by Na+. The results indicate co-transport of Na+ and neutral amino acids inthe human intestinal brush-border membrane.