Results 181 to 190 of about 97,585 (218)
Some of the next articles are maybe not open access.
Structure of pig plasma retinol-binding protein at 1.65 Å resolution
Acta Crystallographica Section D Biological Crystallography, 1998The crystal structure of pig plasma retinol-binding protein (RBP) has been determined at 1.65 A resolution. The space group is P212121, with a = 45.81 (4), b = 53.14 (5), c = 72.97 (8) A and one protein molecule in the asymmetric unit. The structure has been solved using the molecular replacement method and refined with restrained least squares to an R
ZANOTTI G +5 more
openaire +3 more sources
The piscine plasma retinol‐binding protein
European Journal of Biochemistry, 19921. Retinol‐binding protein (RBP) has been isolated from the pooled plasma or rainbow trouts (Oncorhinchus mykiss) by gel filtration, hydrophobic interaction chromatography and ion‐exchange chromatography. By this procedure two forms of the protein, both with a molecular mass (approximately 20 kDa) similar to that of mammalian RBP, were purified to ...
BERNI, Rodolfo, STOPPINI M, ZAPPONI MC
openaire +2 more sources
Journal of Proteome Research, 2003
A human plasma retinol-binding protein (RBP) mutant, named RBP-S, has been designed and produced in which the six native cysteine residues, involved in the formation of three disulfide bonds, have been replaced with serine. A hexa-histidine tag was also added to the C-terminus of RBP for ease of purification. The removal of the disulfide bonds led to a
Gabriel O, Reznik +3 more
openaire +2 more sources
A human plasma retinol-binding protein (RBP) mutant, named RBP-S, has been designed and produced in which the six native cysteine residues, involved in the formation of three disulfide bonds, have been replaced with serine. A hexa-histidine tag was also added to the C-terminus of RBP for ease of purification. The removal of the disulfide bonds led to a
Gabriel O, Reznik +3 more
openaire +2 more sources
Regulation of plasma retinol binding protein secretion in human HepG2 cells
Experimental Cell Research, 1992Retinol binding protein (RBP) is the plasma transport protein of retinol. Mobilization of RBP from the liver stores is stimulated by retinol. During vitamin A deficiency, RBP secretion is specifically inhibited while its rate of biosynthesis is unaffected.
F, Tosetti +4 more
openaire +2 more sources
The partial structure of human plasma prealbumin and retinol-binding protein
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971Abstract A determination of the partial NH 2 -terminal amino acid sequence of human plasma prealbumin suggests that the molecule is a tetramer and that the subunits may have identical, or nearly identical, primary structures. The amino terminal sequence of retinol-binding protein is unrelated.
F J, Morgan, R E, Canfield, D S, Goodman
openaire +2 more sources
Plasma Retinol-Binding Protein in Human Uterine Cervical Dysplasias and Cancer
Gynecologic and Obstetric Investigation, 1989Plasma concentrations of retinol-binding protein (RBP) were measured in a cross-sectional study of asymptomatic normal menstruating women (n = 94) who obtained Pap smears and participated in a double-blinded nutritional survey. Controls (n = 45) were women with negative cervical cytology, normal colposcopy and no known gynecologic pathology or ...
P R, Palan, J, Basu, S L, Romney
openaire +2 more sources
Purification of human plasma retinol-binding protein by hydrophobic interaction chromatography
Analytical Biochemistry, 1985Human plasma retinol-binding protein has been purified to homogeneity by a simple method that requires an ammonium sulfate fractionation, a hydrophobic interaction chromatography on phenyl-Sepharose, which dissociates the complex between retinol-binding protein and its carrier, transthyretin, and a gel filtration on Sephadex G-50.
BERNI, Rodolfo +2 more
openaire +2 more sources
Plasma retinol binding protein: structure and function of the prototypic lipocalin
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000In terms of both structure and biological function, retinol binding protein (RBP) is one of the best characterized members of the lipocalin superfamily. The molecular interactions in which RBP participates are described herein.
M E, Newcomer, D E, Ong
openaire +2 more sources
Circular dichroic studies of human plasma retinol-binding protein and prealbumin
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1972Abstract Circular dichroic (CD) spectra were obtained on solutions of human plasma retinol-binding protein and prealbumin, the two proteins involved in the transport of vitamin A in plasma. CD spectral studies were also carried out on the following solutions: (1) apo-retinol-binding protein (retinol-binding protein not containing bound retinol); (2 ...
A M, Gotto, S E, Lux, D S, Goodman
openaire +2 more sources
Scandinavian Journal of Clinical and Laboratory Investigation, 2000
Plasma retinol-binding protein (RBP) concentrations have been suggested as surrogate indicators for plasma retinol concentrations in the assessment of vitamin A status in less technologically developed settings. Plasma RBP was measured by radial immunodiffusion and plasma retinol by high performance liquid chromatography in a cross-sectional study of ...
J, Almekinder +5 more
openaire +2 more sources
Plasma retinol-binding protein (RBP) concentrations have been suggested as surrogate indicators for plasma retinol concentrations in the assessment of vitamin A status in less technologically developed settings. Plasma RBP was measured by radial immunodiffusion and plasma retinol by high performance liquid chromatography in a cross-sectional study of ...
J, Almekinder +5 more
openaire +2 more sources