Real-time Analyses of Retinol Transport by the Membrane Receptor of Plasma Retinol Binding Protein

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Real-time analyses of retinol transport by the membrane receptor of plasma retinol binding protein.

Vitamin A is essential for vision and the growth/differentiation of almost all human organs. Plasma retinol binding protein (RBP) is the principle and specific carrier of vitamin A in the blood. Here we describe an optimized technique to produce and purify holo-RBP and two real-time monitoring techniques to study the transport of vitamin A by the high-affinity RBP receptor STRA6. The first tech...

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Tissue distribution of the receptor for plasma retinol-binding protein.

The tissue distribution of the retinol-binding-protein receptor has been studied by using a cell-free binding assay. High binding activity was found in placenta, retina pigment epithelial cells, bone marrow and kidneys. Specific binding activity was also found in the small intestines, spleen and liver, and to a lesser extent in lung. Scatchard analysis revealed that the difference in binding ac...

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Radioimmunoassay of human plasma retinol-binding protein.

A radioimmunoassay for human plasma retinol-binding protein (RBP) has been developed utilizing a double antibody precipitation technique. RBP was purified 1500- to 2000-fold by procedures described previously. A specific anti-human RBP antiserum was prepared in rabbits by three once-weekly injections of purified RBP emulsified with Freund's adjuvant. RBP was iodinated with (131)I and the RBP-(1...

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Loss of retinol-binding properties for plasma retinol-binding protein in normal human epidermis.

Terminal differentiation of the keratinocytes (cornification) has been linked to a restricted supply of retinol. Retinol is distributed to target cells by the retinol-binding protein (RBP), which circulates in the plasma in complex with transthyretin (TTR). In this study we have addressed the question of retinol delivery to the epidermis via RBP. Retinol radiobinding assays, affinity chromatogr...

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The interaction of human plasma retinol-binding protein and prealbumin.

The interaction of human plasma retinol-binding protein with plasma prealbumin was studied by the techniques of velocity ultracentrifugation and polarization of retinol fluorescence. In the first method the unbound fraction of retinol-binding protein, which sediments more slowly than its complexes with prealbumin, was measured by its absorption. A stoichiometry of retinol-binding protein to pre...

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ژورنال

عنوان ژورنال: Journal of Visualized Experiments

سال: 2013

ISSN: 1940-087X

DOI: 10.3791/50169