Assessment of binding of L-cystine and L-lysine by rat renal brush-border membranes
Cystine and lysine bind to isolated rat renal brush-border vesicles. Three methods to determine the extent of amino acid binding to the membranes have been compared, one relying on the osmotic reactivity of the vesicle, a second by trichloroacetic acid precipitation of membrane-bound material and a...
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Published in: | Biochimica et biophysica acta Vol. 863; no. 2; p. 332 |
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Main Authors: | , , , , |
Format: | Journal Article |
Language: | English |
Published: |
Netherlands
16-12-1986
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Subjects: | |
Online Access: | Get more information |
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Summary: | Cystine and lysine bind to isolated rat renal brush-border vesicles. Three methods to determine the extent of amino acid binding to the membranes have been compared, one relying on the osmotic reactivity of the vesicle, a second by trichloroacetic acid precipitation of membrane-bound material and a third by initial rate analysis. For cystine, all methods yield comparable results at early time points, indicating the trichloroacetic acid method is a simple and valuable tool for binding estimation under initial-rate or near initial-rate conditions. For lysine, initial rate analysis and osmotic perturbation are the methods of choice since lysine co-precipitates with trichloroacetic acid. |
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ISSN: | 0006-3002 |
DOI: | 10.1016/0005-2736(86)90277-4 |