Results 161 to 170 of about 21,717 (210)
Some of the next articles are maybe not open access.
Porcine retinol binding protein
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1972Abstract 1. 1. The retinol binding protein (RBP) in porcine serum was partially purified and characterized. 2. 2. Purification was by Cohn fractionation, filtration on Sephadex G-200, chromatography on DEAE Sephadex A-50 and preparative polyacrylamide electrophoresis. 3. 3.
C C, Huang, R E, Howarth, B D, Owen
openaire +2 more sources
Cellular retinol-binding protein
Biochimica et Biophysica Acta (BBA) - General Subjects, 19751. A protein which binds retinol in vitro with high affinity and specificity was detected by sucrose gradient centrifugation or by gel filtration after preincubating rat tissue cytosols with all-trans-[3H]retinol. This protein sediments in the 2 S region of sucrose gradients.
M M, Bashor, F, Chytil
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
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
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
openaire +2 more sources
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
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
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
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

