Results 261 to 270 of about 55,898 (311)
Some of the next articles are maybe not open access.
Prealbumin-retinol-binding-protein-retinol complex in hemodialysis patients
The American Journal of Clinical Nutrition, 1988In hemodialysis (HD) patients, serum prealbumin (TBPA) is correlated to nutritional status and outcome despite usually elevated serum levels. The purpose of this work was to study the role of TBPA-retinol-binding-protein (RBP)-retinol complex changes in the elevation of serum TBPA in HD patients.
N, Cano +7 more
openaire +2 more sources
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.
openaire +2 more sources
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 ...
openaire +2 more sources
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 ...
openaire +2 more sources
Biochemistry, 1992
The interactions within the molecular complex in which retinol circulates in blood were studied. To monitor binding between retinol-binding protein (RBP) and transthyretin (TTR), TTR was labeled with a long-lived fluorescence probe (pyrene). Changes in the rotational volume of TTR following its association with RBP were monitored by fluorescence ...
N, Noy, E, Slosberg, S, Scarlata
openaire +2 more sources
The interactions within the molecular complex in which retinol circulates in blood were studied. To monitor binding between retinol-binding protein (RBP) and transthyretin (TTR), TTR was labeled with a long-lived fluorescence probe (pyrene). Changes in the rotational volume of TTR following its association with RBP were monitored by fluorescence ...
N, Noy, E, Slosberg, S, Scarlata
openaire +2 more sources
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
openaire +2 more sources
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
openaire +1 more source
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
openaire +1 more source
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 ...
openaire +2 more sources
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
openaire +1 more source
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
openaire +1 more source
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
openaire +1 more source
Aspects of the Metabolism of Retinol-Binding Protein and Retinol
1975Publisher Summary This chapter presents different aspects of the metabolism of retinol-binding protein (RBP) and retinol. RBP is not significantly decreased until the liver reserves of the vitamin are virtually abolished. The diminished concentration of RBP in plasma in manifest vitamin A deficiency reflects the impaired transport of retinol to the ...
P A, Peterson +4 more
openaire +2 more sources