Conformational Changes following Interaction between Retinol Isomers and Human Retinol-binding Protein and between the Retinol-binding Protein and Prealbumin
نویسندگان
چکیده
منابع مشابه
The interaction of human plasma retinol-binding protein and prealbumin.
The interaction of human plasma retinol-binding protein with plasma prealbumin was studied by the techniques of velocity ultracentrifugation and polarization of retinol fluorescence. In the first method the unbound fraction of retinol-binding protein, which sediments more slowly than its complexes with prealbumin, was measured by its absorption. A stoichiometry of retinol-binding protein to pre...
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In hemodialysis (HD) patients, serum prealbumin (TBPA) is correlated to nutritional status and outcome despite usually elevated serum levels. The purpose of this work was to study the role of TBPA-retinol-binding-protein (RBP)-retinol complex changes in the elevation of serum TBPA in HD patients. Serum TBPA, RBP, and retinol were measured in 30 otherwise healthy HD patients (15 men, 15 women) a...
متن کاملThe interaction of thyroxine with human plasma prealbumin and with the prealbumin-retinol-binding protein complex.
Prealbumin was isolated from human plasma by chromatography on columns of diethylaminoethyl Sephadex and Sephadex G-200, followed by preparative polyacrylamide gel electrophoresis. The prealbumin was homogeneous in the analytical ultracentrifuge with an s=z~,~ of 3.7 S and with a molecular weight of about 50,000. Prealbumin formed a protein-protein complex with plasma retinol-binding protein in...
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Vitamin A (retinol) is required to maintain immunity and epithelial turnover and is a key micronutrient needed for combating infection. Vitamin A actions on the immune system are diverse and cannot be accounted for by a single effect or mechanism. The actions of retinol in maintaining gut integrity in humans and immunoglobulin levels in mice was investigated. For 30 children, performance on the...
متن کاملBinding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics.
The structure and backbone dynamics of rat holo cellular retinol-binding protein II (holo-CRBP II) in solution has been determined by multidimensional NMR. The final structure ensemble was based on 3980 distance and 30 dihedral angle restraints, and was calculated using metric matrix distance geometry with pairwise Gaussian metrization followed by simulated annealing. The average RMS deviation ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)43449-2