Involvement of tyrosine and lysine residues of retinol-binding protein in the interaction between retinol and retinol-binding protein and between retinol-binding protein and prealbumin. Acetylation with N-acetylimidazole and alkaline titration.
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چکیده
منابع مشابه
Prealbumin-retinol-binding-protein-retinol complex in hemodialysis patients.
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 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...
متن کاملRetinol and retinol-binding protein: gut integrity and circulating immunoglobulins.
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 کاملModification of tryptophan residues in retinol-binding protein and prealbumin with 2-hydroxy-5-nitrobenzyl bromide. Effects of the modification of the protein-retinol and protein-protein interaction.
Human retinol-binding protein (RBP) and prealbumin were labeled with Z-hydroxy&nitrobenzyl bromide (HNB-Br) at pH 5.5 using 20to loo-fold molar excess of the label over tryptophan in each protein. In prealbumin, only 1 to 1.7 tryptophan residues out of 8 were modified under these conditions. This modification did not alter the capacity of prealbumin to bind to retinol-RBP at physiological ionic...
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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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1975
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)41588-3