Binding Affinities of Retinol and Related Compounds to Retinol Binding Proteins
TLDR
The above results suggest that both human and chicken retinol binding proteins behave similar with respect to the binding of the ligands.Citations
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Journal ArticleDOI
The lipocalin protein family: structure and function
TL;DR: It is now clear that the lipocalins exhibit great functional diversity, with roles in retinol transport, invertebrate cryptic coloration, olfaction and pheromone transport, and prostaglandin synthesis.
Journal ArticleDOI
Effects of vitamin A and its analogs (retinoids) on normal and neoplastic cells
Journal ArticleDOI
The structure of β -lactoglobulin and its similarity to plasma retinol-binding protein
Miroslav Z. Papiz,Lindsay Sawyer,Elias Eliopoulos,Anthony C.T. North,John B. C. Findlay,R. Sivaprasadarao,T.A. Jones,M. E. Newcomer,P. J. Kraulis +8 more
TL;DR: A possible binding site for retinol in BLG has been identified by model-building and a role for BLG in vitamin A transport is suggested and specific receptors for the BLG–retinol complex in the intestine of neonate calves are discovered.
Journal ArticleDOI
Interaction of β-Lactoglobulin with Resveratrol and its Biological Implications
TL;DR: In this article, the interaction of resveratrol with beta-lactoglobulin was investigated using circular dichroism, fluorescence and UV-vis absorbance, and the binding constant for the 2-way interaction was found to be between 10(4 and 10(6) M (-1), as determined by protein or polyphenol fluorescence.
Journal ArticleDOI
Plasma Retinol-Binding Protein
TL;DR: These findings reflect the facts that RBP is produced in the liver and mainly catabolized in the kidneys, and delivery of retinol to extra-hepatic tissues appears to involve specific cell surface receptors for RBP.
References
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Journal ArticleDOI
Correction of fluorescence spectra and measurement of fluorescence quantum efficiency
C. A. Parker,W. T. Rees +1 more
Journal ArticleDOI
Retinol-binding protein: the transport protein for vitamin A in human plasma
TL;DR: In plasma, RBP apparently circulates as a complex, together with another, larger protein with prealbumin mobility on electrophoresis, which appears to involve both a lipid-protein (retinol-RBP) interaction and a protein- protein (RBP-prealbumin) interaction.
Journal ArticleDOI
The Enhancement of Fluorescence and the Decreased Susceptibility to Enzymatic Oxidation of Retinol Complexed with Bovine Serum Albumin, β-Lactoglobulin, and the Retinol-binding Protein of Human Plasma
Sidney Futterman,Joram Heller +1 more
TL;DR: The greater degree of fluorescence enhancement, the greater stability ofretinol in RBP and PA-RBP to spontaneous degradation at room temperature, the relative resistance to extraction of the bound retinol by ether, and the complete unavailability of the retinols inRBP andPA-R BP for oxidation by liver alcohol dehydrogenase were interpreted as indicating that retinOL is bound with greater affinity to the natural carrier protein than it is to bovine serum albumin or
Journal ArticleDOI
Extraction and recombination studies of the interaction of retinol with human plasma retinol-binding protein
DeWitt S. Goodman,Amiram Raz +1 more
TL;DR: The recombination procedure was employed to examine the specificity of the binding of retinol to RBP, by determining whether compounds other than all-trans-retinol would effectively bind to apo-RBP.
Book ChapterDOI
[41] Assay and properties of corticosteroid-binding globulin and other steroid-binding serum proteins
TL;DR: This chapter describes methods that are used to determine the various binding parameters involved in the interaction of steroids with serum proteins.
Related Papers (5)
The Enhancement of Fluorescence and the Decreased Susceptibility to Enzymatic Oxidation of Retinol Complexed with Bovine Serum Albumin, β-Lactoglobulin, and the Retinol-binding Protein of Human Plasma
Sidney Futterman,Joram Heller +1 more