Results 171 to 180 of about 21,755 (220)
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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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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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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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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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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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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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Retinol-Binding Proteins in Human Testis Cytosol
The Journal of Nutrition, 1978In the cytosol fraction of human testes a specific binding protein for retinol has been isolated by sephadex column chromatography and by gradient centrifugation. The protein has a sedimentation coefficient of 2S, and its molecular weight is estimated by gel filtration to be approximately 16,000 daltons. Competitive binding studies with labeled retinol
G S, Ahluwalia +2 more
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