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Purification of Human Plasma Retinol-Binding Protein by Hydrophobic Interaction Chromatography
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Crystal Structure of the Trigonal Form of Human Plasma Retinol-Binding Protein at 2.5 Å Resolution.
No full textHuman plasma retinol-binding protein (RBP4) is also a fatty acid-binding protein
Full text linkRBP4 (plasma retinol-binding protein) is the 21 kDa transporter of all-trans retinol that circulates in plasma as a moderately tight 1:1 molar complex of the vitamin with the protein. RBP4 is primarily synthesised in the liver but is also produced by adipose tissue and circulates bound to a larger protein, transthyretin, TTR, that serves to increase its molecular mass and thus avoid its elimination by glomerular filtration. This paper reports the high resolution three-dimensional structures of human RBP4 naturally lacking bound retinol purified from plasma, urine and amniotic fluid. In all these crystals we found a fatty acid molecule bound in the hydrophobic ligand-binding site, a result confirmed by mass spectrometry measurements. In addition we also report the 1.5 Å resolution structures of human holo-RBP4 and of the protein saturated with palmitic and lauric acid and discuss the interaction of the fatty acids and retinol with the protein
PROBING PROTEIN AGGREGATION BY TIME-RESOLVED FLUORESCENCE DURING BETA-LACTOGLOBULIN CRYSTAL GROWTH
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Bovine Plasma Retinol-Binding Protein: Amino Acid Sequence, Interaction with Transthyretin, Crystallization and Preliminary X-Ray Data
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