Results 241 to 250 of about 5,652,471 (282)
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Serum Retinol and Retinol-Binding Protein in Mothers and Infants at Delivery
Biology of the Neonate, 2009The relations at birth between infant and maternal serum retinol, retinol-binding protein (RBP) and retinol/RBP molar ratio were investigated in 25 healthy term infants and their mothers. The mean serum levels of retinol and RBP were significantly higher in the mothers, but the mean molar ratio of retinol/RBP (RBP saturation) was significantly higher ...
L, Jansson, B, Nilsson
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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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Scandinavian journal of clinical and laboratory investigation. Supplementum, 1981
Vitamin A is transported from its storage site in the liver to the epithelial tissues by a carrier protein, the Retinol-binding protein (RBP). In plasma RBP forms a complex with thyroxine-binding prealbumin. The present article reviews available data on the RBP system. The complete primary structure of RBP has been determined.
L, Rask +8 more
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Vitamin A is transported from its storage site in the liver to the epithelial tissues by a carrier protein, the Retinol-binding protein (RBP). In plasma RBP forms a complex with thyroxine-binding prealbumin. The present article reviews available data on the RBP system. The complete primary structure of RBP has been determined.
L, Rask +8 more
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The transthyretin-retinol-binding protein complex
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000Transthyretin (TTR, formerly called prealbumin), one of the transporters of the hormone thyroxine and the lipocalin retinol-binding protein (RBP), the specific carrier of the vitamin, are known to form, under physiological conditions, a macromolecular complex that is believed to play an important physiological role: prevention of glomerular filtration ...
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Retinoids: in vitro interaction with retinol‐binding protein and influence on plasma retinol
The 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 ...
BERNI, Rodolfo +4 more
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Retinol and retinol-binding protein in neonates with Bronchopulmonary Dysplasia
Nutrition Research, 1999Abstract The incidence of Bronchopulmonary Dysplasia (BPD) is high in preterm very-low-birth-weight infants, and prematurity is one the main causes of neonatal and infant morbidity and mortality in Mexico. The objective of the study was to evaluate vitamin A status of infants at risk for BPD.
Roxana Valdés-Ramos +4 more
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Archives of Biochemistry and Biophysics, 1985
Retinol (vitamin A alcohol), which plays an important role in the differentiation of epithelia, can be transferred to chromatin in vitro. Rat liver chromatin can accept retinol in a specific and saturable manner only when the retinol is presented as a complex with cellular retinol-binding protein (CRBP).
G, Liau, D E, Ong, F, Chytil
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Retinol (vitamin A alcohol), which plays an important role in the differentiation of epithelia, can be transferred to chromatin in vitro. Rat liver chromatin can accept retinol in a specific and saturable manner only when the retinol is presented as a complex with cellular retinol-binding protein (CRBP).
G, Liau, D E, Ong, F, Chytil
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1995
Retinol binding protein is a single chain polypeptide of 21 000 Da without associated carbohydrate. It is the sole transport protein for vitamin A, and exists in the serum as an equimolar complex with prealbumin (trans-thyretin). Free retinol binding protein is rapidly excreted by the kidney, the function of the prealbumin-RBP complex appearing to be a
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Retinol binding protein is a single chain polypeptide of 21 000 Da without associated carbohydrate. It is the sole transport protein for vitamin A, and exists in the serum as an equimolar complex with prealbumin (trans-thyretin). Free retinol binding protein is rapidly excreted by the kidney, the function of the prealbumin-RBP complex appearing to be a
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Thermodynamic parameters of the binding of retinol to binding proteins and to membranes
Biochemistry, 1990Retinol (vitamin A alcohol) is a hydrophobic compound and distributes in vivo mainly between binding proteins and cellular membranes. To better clarify the nature of the interactions of retinol with these phases which have a high affinity for it, the thermodynamic parameters of these interactions were studied. The temperature-dependence profiles of the
N, Noy, Z J, Xu
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Serum retinol binding protein 4 contributes to insulin resistance in obesity and type 2 diabetes
Nature, 2005Qin Yang +8 more
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