Results 161 to 170 of about 21,720 (214)
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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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1974
Publisher Summary This chapter discusses the methods of isolation, chemical nature, physical properties, biochemistry, and methods of assay of retinol-binding proteins (RBP). The discovery of the importance of vitamin A (retinol) and of the animal in preventing night blindness and maintaining normal growth of the animal body, in replacement of ...
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Publisher Summary This chapter discusses the methods of isolation, chemical nature, physical properties, biochemistry, and methods of assay of retinol-binding proteins (RBP). The discovery of the importance of vitamin A (retinol) and of the animal in preventing night blindness and maintaining normal growth of the animal body, in replacement of ...
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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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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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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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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.
N, Noy, W S, 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.
N, Noy, W S, Blaner
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Multiple retinol binding proteins in rabbit lung
Biochemical and Biophysical Research Communications, 1974Summary Rabbit lungs contain components sedimenting on sucrose gradients with a sedimentation coefficient of 2S that bind retinol with high specificity. DEAE-cellulose chromatography following gel filtration reveals the presence of 3 binding components of 17,000, 15,000 and 14,000 daltons respectively, showing different fluorescence spectra.
D E, Ong, F, Chytil
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Characterization of retinol-binding protein in familial hypo-retinol-binding proteinemia.
Japanese journal of ophthalmology, 1989We reported previously familial hypo-retinol-binding proteinemia in a child who developed keratomalacia during measles infection. In the present study, we characterized serum retinol-binding proteins (RBPs) in the affected family members and compared these RBPs with those in the unaffected family members. Immunoblotting following SDS-polyacrylamide gel
T, Matsuo, N, Matsuo
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Study of retinol-binding protein in pancreatic cancer
Journal of Cancer Research and Clinical Oncology, 1984Serum RBP, prealbumin, and zinc were evaluated in normal subjects and patients with pancreatic cancer and chronic pancreatitis. A significant decrease of RPB was found in pancreatic cancer patients compared with controls. A concomitant reduction of prealbumin and zinc was also observed.
FABRIS C. +8 more
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