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- W1717786074 abstract "A procedure for the synthesis of tritiated 4-azidophenylalanine in a radioactively homogeneous form is described. The characteristics of the 4-azidophenylalanine uptake by pig intestinal microvillar vesicles and its interaction with the neutral amino acid transport have been studied. 4-Azidophenylalanine is transported into an osmotically sensitive space and the transport is sodium dependent. It is demonstrated that 4-azidophenylalanine transport is inhibited by L-alanine and L-phenylalanine but not by L-lysine and D-glucose. Likewise 4-azidophenylalanine inhibited the initial transport of L-alanine and L-phenylalanine but the initial transport of L-lysine and D-glucose was unaffected. Treatment of microvillar vesicles with 4-azidophenylalanine in combination with photolysis irreversibly inactivated the L-alanine transport. Photolabelling in the presence of sodium using tritiated 4-azidophenylalanine resulted in labelling of 10 peptides, all found in the fraction insoluble in Triton X-100. Omission of sodium from the reaction mixture or addition of L-alanine did not specifically abolish labelling in any of the labelled components." @default.
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- W1717786074 date "1983-07-01" @default.
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- W1717786074 title "Na+-Dependent Uptake of 4-Azidophenylalanine by Pig Intestinal Microvillus Vesicles. Interaction with Neutral Amino Acid Uptake and Labelling Pattern" @default.
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- W1717786074 doi "https://doi.org/10.1111/j.1432-1033.1983.tb07532.x" @default.
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