Abstract
It is not difficult to understand the need for a carrier for retinol in plasma since the molecule is not soluble in an aqueous medium. The protein that effects this function is called plasma Retinol-Binding Protein (RBP) (for a recent review see reference 1). Two other additional functions are performed by this protein: protection of the labile retinol molecule and selective delivery, since the vitamin is only transferred from the carrier to the cells that have a specific membrane receptor (2,3). Retinol-Binding Proteins have been characterized in the plasma of many species including man. The retinol transport system in human plasma includes another well known protein, transthyretin, formerly known as prealbumin. The two proteins form, under physiological conditions, a one to one complex that has an enhanced tendency to dissociate upon delivery of the vitamin to the receptors. Other conditions that favor dissociation are low ionic strength (4) and perhaps disruption of hydrophobic contacts (5).
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Monaco, H.L., Zanotti, G., Spadon, P. (1987). Crystallographic Studies on Retinol-Binding Protein and Beta Lactoglobulin. In: Chaiken, I., Chiancone, E., Fontana, A., Neri, P. (eds) Macromolecular Biorecognition. Experimental Biology and Medicine, vol 19. Humana Press. https://doi.org/10.1007/978-1-4612-4600-8_5
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DOI: https://doi.org/10.1007/978-1-4612-4600-8_5
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