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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Bibliographic Details
Published in:Biochimica et biophysica acta Vol. 863; no. 2; p. 332
Main Authors: Hsu, B Y, McNamara, P D, Rea, C T, Corcoran, S M, Segal, S
Format: Journal Article
Language:English
Published: Netherlands 16-12-1986
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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.
ISSN:0006-3002
DOI:10.1016/0005-2736(86)90277-4