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. 1992 Feb 15;282(Pt 1):123–128. doi: 10.1042/bj2820123

Direct zinc binding to purified rhodopsin and disc membranes.

T A Shuster 1, A K Nagy 1, D C Conly 1, D B Farber 1
PMCID: PMC1130898  PMID: 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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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