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Biochemistry, 1991
The interactions of retinol with rat cellular retinol-binding protein (CRBP) and with rat serum retinol-binding protein (RBP) were studied. The equilibrium dissociation constants of the two retinol-protein complexes (Kd) were found to be 13 x 10(-9) and 20 x 10(-9) M for CRBP and for RBP, respectively.
Noa Noy, William Blaner
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The interactions of retinol with rat cellular retinol-binding protein (CRBP) and with rat serum retinol-binding protein (RBP) were studied. The equilibrium dissociation constants of the two retinol-protein complexes (Kd) were found to be 13 x 10(-9) and 20 x 10(-9) M for CRBP and for RBP, respectively.
Noa Noy, William Blaner
exaly +3 more sources
Porcine retinol binding protein
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1972Abstract 1. 1. The retinol binding protein (RBP) in porcine serum was partially purified and characterized. 2. 2. Purification was by Cohn fractionation, filtration on Sephadex G-200, chromatography on DEAE Sephadex A-50 and preparative polyacrylamide electrophoresis. 3. 3.
C C, Huang, R E, Howarth, B D, Owen
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Cellular retinol-binding protein
Biochimica et Biophysica Acta (BBA) - General Subjects, 19751. A protein which binds retinol in vitro with high affinity and specificity was detected by sucrose gradient centrifugation or by gel filtration after preincubating rat tissue cytosols with all-trans-[3H]retinol. This protein sediments in the 2 S region of sucrose gradients.
M M, Bashor, F, Chytil
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Expression of retinol‐binding protein and cellular retinol‐binding protein in the bovine ovary
Molecular Reproduction and Development, 2003AbstractRetinol (vitamin A) is essential for reproduction, and retinoids have been suggested to play a role in ovarian steroidogenesis, oocyte maturation, and early embryonic development. Retinol is transported systemically and intercellularly by retinol‐binding protein (RBP).
J Alison, Brown +4 more
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PLASMA RETINOL‐BINDING PROTEIN*
Annals of the New York Academy of Sciences, 1980Vitamin A is mobilized from liver stores and transported in plasma in the form of the lipid alcohol retinol, bound to a specific transport protein, retinol-binding protein (RBP). A great deal is known about the chemical structure, metabolism, and biological roles of RBP. RBP is a single polypeptide chain with molecular weight close to 20,000.
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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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Retinol‐Binding Protein and Prealbumin
Journal of Pediatric Gastroenterology and Nutrition, 1986SummaryPlasma prealbumin (PA) and retinol‐binding protein (RBP) concentrations were serially measured in 25 critically ill, malnourished infants requiring parenteral nutrition to determine if these visceral protein markers are useful in assessing acute protein repletion. Significant increases in both proteins (p > 0.05) were noted as early as 5 to 7
Richard A. Helms +4 more
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