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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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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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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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Pityriasis rubra pilaris and retinol-binding protein
British Journal of Dermatology, 1981Serum levels of retinol-binding protein (the specific carrier of vitamin A) were measured in eleven patients with pityriasis rubra pilaris and in some of their close relatives. The level of retinol-binding protein was markedly reduced in every patient, and in some of the relatives. It is postulated that defective synthesis of retinol-binding protein is
A F, Finzi +3 more
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Retinol binding protein and prealbumin in Reye's Syndrome
Clinical Biochemistry, 1986Retinol binding protein (RBP) and prealbumin (PA) were analyzed in 29 serum samples from 8 patients with stages II and III Reye's Syndrome (RS), and from 10 healthy fasting children. All RS patients had at least one abnormally low RBP and PA value. A return toward normal was evident within 2-3 days in serial samples.
E, Bosin, A M, Glasgow, N, Monji
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Distribution of Retinol-Binding Prctein in Tissues
1975Publisher Summary This chapter discusses the distribution of retinol-binding protein (RBP) in tissues. Serial sections of pig and human liver tissue obtained shortly post mortem were fixed in ethanol and treated with unlabeled specific rabbit antiserum to human RBP. The pig RBP cross reacts to a considerable extent with human antiserum.
J, Glover, C, Jay, G H, White
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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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RETINOL-BINDING PROTEIN IN MALNUTRITION
The Lancet, 1979W A, Coward, P G, Lunn
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