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Sulfhydyl group involvement in the modulation of neutral amino acid transport in thymocyte membrane vesicles
Author(s) -
Kwock Lester
Publication year - 1981
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041060214
Subject(s) - glutathione , chemistry , aminoisobutyric acid , amino acid , vesicle , membrane , biochemistry , reagent , thymocyte , biophysics , biology , enzyme , antigen , cd8 , genetics
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.