Results 171 to 180 of about 97,585 (218)

Sex Differences in Vitamin Metabolism and Their Role in Oxidative Stress Regulation and Cardiometabolic Health. [PDF]

open access: yesNutrients
Wróblewska J   +5 more
europepmc   +1 more source

Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein

Science, 1995
The three-dimensional structure of the complex formed by two plasma proteins, transthyretin and retinol-binding protein, was determined from x-ray diffraction data to a nominal resolution of 3.1 angstroms. One tetramer of transthyretin was bound to two molecules of retinol-binding protein. The two retinol-binding protein molecules established molecular
MONACO, Ugo Luigi, M. Rizzi, A. Coda
openaire   +4 more sources

Structure of chicken plasma retinol-binding protein

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2001
The crystal structure of the specific carrier of retinol (retinol-binding protein, RBP) purified from chicken plasma has been determined (space group P2(1)2(1)2(1), with a=46.06(5) A, b=53.56(6) A, c=73.41(8) A, and one protein molecule in the asymmetric unit). Despite being obtained from a species phylogenetically distant from mammals, chicken holoRBP
Giuseppe Zanotti   +5 more
openaire   +3 more sources

Crystallization of human plasma apo-retinol-binding protein

Journal of Molecular Biology, 1984
Crystals of three forms of human plasma apo-retinol-binding protein have been obtained using the procedure described for the holoprotein. The apoprotein was prepared by a novel method, which uses hydrophobic interaction and immobilized dye chromatography. The three forms were separated by fast protein liquid chromatography.
MONACO HL   +3 more
openaire   +2 more sources

Fluorescence studies of human plasma retinol-binding protein and of the retinol-binding protein-prealbumin complex

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

Plasma Retinol Binding Protein for Monitoring the Acetaminophen-induced Hepatotoxicity

Drug Metabolism and Pharmacokinetics, 2002
Retinol-binding protein (RBP) is a specific transport protein which carries retinol in the circulation. RBP concentration in plasma and liver of rats following a large dose of acetaminophen (APAP) intraperitoneally was examined. The RBP concentration in plasma decreased significantly at 12 hr after the APAP administration, while the plasma albumin ...
Masanao, Isozaki   +3 more
openaire   +2 more sources

PLASMA RETINOL‐BINDING PROTEIN*

Annals of the New York Academy of Sciences, 1980
Vitamin 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

Production of human plasma retinol-binding protein in Escherichia coll

Gene, 1993
We designed a polymerase chain reaction (PCR) primer pair which allowed us to clone the cDNA coding for the human plasma retinol-binding protein (hRBP) into an Escherichia coli expression vector. Production of hRBP was confirmed by probing Western blots with antisera against plasma hRBP. Purification and characterization of the E.
T T, Wang, K C, Lewis, J M, Phang
openaire   +2 more sources

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