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Veterinary Journal, 2006 The aim of this study was to investigate differences in concentrations of vitamin A, transthyretin (TTR) and retinol-binding protein (RBP) between plasma and cerebrospinal fluid (CSF) in dogs. RBP was detected using ELISA, and both RBP and TTR by Western blot analysis after separation on SDS-PAGE.
Florian J. Schweigert, Leo Brunnberg
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Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein
Science, 1995 The three-dimensional structure of the complex formed by two plasma proteins, transthyretin and retinol-binding protein, was determined from x-ray diffraction data to a nominal resolution of 3.1 angstroms. One tetramer of transthyretin was bound to two molecules of retinol-binding protein. The two retinol-binding protein molecules established molecular
MONACO, Ugo Luigi, M. Rizzi, A. Coda
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Structure of chicken plasma retinol-binding protein
BBA - Proteins and Proteomics, 2001The crystal structure of the specific carrier of retinol (retinol-binding protein, RBP) purified from chicken plasma has been determined (space group P2(1)2(1)2(1), with a=46.06(5) A, b=53.56(6) A, c=73.41(8) A, and one protein molecule in the asymmetric unit). Despite being obtained from a species phylogenetically distant from mammals, chicken holoRBP
Giuseppe Zanotti +2 more
exaly +5 more sources
Retinoids: in vitro interaction with retinol-binding protein and influence on plasma retinol
FASEB Journal, 1993Studies have been conducted to investigate the structure‐function relationships of retinoids in their in vitro interaction with plasma retinol‐binding protein (RBP) and in their influence on plasma retinol concentration. Two classes of retinoids, one bearing modifications in the area of the retinol hydroxyl end group (fenretinide ...
Rodolfo Berni +2 more
exaly +4 more sources
Purification of human plasma retinol-binding protein by hydrophobic interaction chromatography
Analytical Biochemistry, 1985Human plasma retinol-binding protein has been purified to homogeneity by a simple method that requires an ammonium sulfate fractionation, a hydrophobic interaction chromatography on phenyl-Sepharose, which dissociates the complex between retinol-binding protein and its carrier, transthyretin, and a gel filtration on Sephadex G-50.
Simone Ottonello +2 more
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Biochimica Et Biophysica Acta - General Subjects, 1979 The mechanism underlying homeostatic regulation of the plasma levels of free retinol-binding protein and free thyroxine, the systemic distribution of which is of great importance, has been investigated. A simple method has been developed to determine the
H R Cama
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Crystallization of human plasma apo-retinol-binding protein
Journal of Molecular Biology, 1984Crystals of three forms of human plasma apo-retinol-binding protein have been obtained using the procedure described for the holoprotein. The apoprotein was prepared by a novel method, which uses hydrophobic interaction and immobilized dye chromatography. The three forms were separated by fast protein liquid chromatography.
MONACO HL +3 more
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Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1972
Abstract Fluorescence excitation and emission spectra were recorded for human plasma retinol-binding protein and for the complex of retinol-binding protein and prealbumin. The spectra were compared with the fluorescence spectra of retinol in solution in seven different organic solvents.
D S, Goodman, R B, Leslie
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Abstract Fluorescence excitation and emission spectra were recorded for human plasma retinol-binding protein and for the complex of retinol-binding protein and prealbumin. The spectra were compared with the fluorescence spectra of retinol in solution in seven different organic solvents.
D S, Goodman, R B, Leslie
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Structure of pig plasma retinol-binding protein at 1.65 Å resolution
Acta Crystallographica Section D Biological Crystallography, 1998The crystal structure of pig plasma retinol-binding protein (RBP) has been determined at 1.65 A resolution. The space group is P212121, with a = 45.81 (4), b = 53.14 (5), c = 72.97 (8) A and one protein molecule in the asymmetric unit. The structure has been solved using the molecular replacement method and refined with restrained least squares to an R
ZANOTTI G +5 more
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The partial structure of human plasma prealbumin and retinol-binding protein
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971Abstract A determination of the partial NH 2 -terminal amino acid sequence of human plasma prealbumin suggests that the molecule is a tetramer and that the subunits may have identical, or nearly identical, primary structures. The amino terminal sequence of retinol-binding protein is unrelated.
F J, Morgan, R E, Canfield, D S, Goodman
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