Work

Assessment of binding of l-cystine and l-lysine by rat renal brush-border membranes

Year: 1986

Type: article

Abstract: 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.

Source: Biochimica et Biophysica Acta (BBA) - Biomembranes

DOI: 10.1016/0005-2736(86)90277-4

Authors: Betty Y.L. Hsu, Pamela D. McNamara, Claire T. Rea, Susan M. Corcoran, Stanton Segal

Institutions: Children's Hospital of Philadelphia, University of Pennsylvania

Language: English

Topic: Amino Acid Enzymes and Metabolism

Subfield: Biochemistry

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,870

Funder: National Institutes of Health