Sulfhydyl group involvement in the modulation of neutral amino acid transport in thymocyte membrane vesicles

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Abstract
Membrane vesicles from rat thymocytes accumulate 2‐aminoisobutyric acid in the presence of 0.1 M NaCl. Uptake is half maximal between 15 and 30 seconds after addition of the amino acid and reaches a plateau value after about 2 minutes. The uptake of 2‐aminoisobutyric acid can be modulated by various sulfhydryl reagents. Reduced glutathione leads to an inhibition of uptake whereas oxidized glutathione increases uptake. Agents such as insulin and diamide which can induce disulfide formation lead to an activation of transport. These data indicate that uptake of the Na+‐dependent amino acid, 2‐aminoisobutyric acid, in thymocytes is modulated by a putative plasma membrane, sulfhydryl‐containing protein.