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Reconstitution of neutral amino acid transport from partially purified membrane components from ehrlich ascites tumor cells

✍ Scribed by Cecchini, Gary ;Payne, Gregory S. ;Oxender, Dale L.

Publisher
Wiley (John Wiley & Sons)
Year
1977
Tongue
English
Weight
430 KB
Volume
7
Category
Article
ISSN
0091-7419

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✦ Synopsis

Abstract

Solubilized protein fractions have been obtained from plasma membranes of Ehrlich ascites cells either by extraction with 0.5% Triton X‐100 or by extraction with 2% cholate. Partial purification of the solubilized protein fraction has been obtained by utilizing a combination of ammonium sulfate precipitation and column chromatography. Leucine‐binding activity has been detected in the Triton X‐100 solubilized membrane fraction. The leucine‐binding activity was measured by equilibrium dialysis and was saturable with high levels of leucine or phenylalanine and is not strongly effected by alanine. These properties are similar to those previously identified as System L. In addition, the cholate extracted protein fraction was partially purified and reconstituted into liposomes. Sodium dependent uptake of alanine and leucine could be demonstrated in the reconstituted vesicles. Concentrative uptake was dependent upon a sodium gradient. A membrane potential produced by valinomycin mediated potassium diffusion in the presence of sodium also stimulated amino acid transport in reconstituted liposomes.

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Uptake of amino acids in reconstituted v
Uptake of amino acids in reconstituted vesicles derived from plasma membranes of ehrlich ascites cells
✍ R. M. Johnstone; Claudette Bardin 📂 Article 📅 1976 🏛 John Wiley and Sons 🌐 English ⚖ 357 KB

## Abstract To obtain a clearer concept of the mechanism of organic solute transport in mammalian cells, we have attempted to reconstitute a functional transport system for amino acids from plasma membranes of Ehrlich ascites cells. Purified plasma membranes were dissolved in 2% Na cholate—4 M urea

Transport of amino acids in intact 3T3 a
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✍ Cecchini, Gary ;Lee, Mary ;Oxender, Dale L. 📂 Article 📅 1976 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 315 KB

## Abstract Transport of amino acids into 3T3 and SV3T3 (SV40 virus‐transformed 3T3) cells was measured on glass cover slips. The 3T3 and SV3T3 cells contain both A (alanine preferring) and L (leucine preferring) systems for neutral amino acid transport. Initial rates of uptake of amino acids are a