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  • Title: Direct zinc binding to purified rhodopsin and disc membranes.
    Author: Shuster TA, Nagy AK, Conly DC, Farber DB.
    Journal: Biochem J; 1992 Feb 15; 282 ( Pt 1)(Pt 1):123-8. PubMed ID: 1540127.
    Abstract:
    Using the radionuclide 65Zn, we have demonstrated the direct binding of zinc to purified rhodopsin. 65Zn is eluted with detergent-solubilized rhodopsin from concanavalin A columns and remains bound to the visual pigment through a subsequent gel-filtration step. Zinc binding to purified disc membranes is highly specific and, of the ions tested, copper is the best competitor. Equilibrium-dialysis experiments indicate that zinc binding to detergent-solubilized forms of rhodopsin may increase on bleaching the photopigment. These results may have important implications for studies that indicate that zinc plays a role in retinal degeneration and normal photoreceptor physiology.
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