Results 171 to 180 of about 22,170 (210)
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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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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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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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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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