Unknown

Dataset Information

0

Direct zinc binding to purified rhodopsin and disc membranes.


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.

SUBMITTER: Shuster TA 

PROVIDER: S-EPMC1130898 | biostudies-other | 1992 Feb

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC7577997 | biostudies-literature
| S-EPMC3261860 | biostudies-literature
| S-EPMC2584695 | biostudies-literature
| S-EPMC3044992 | biostudies-literature
| S-EPMC2660604 | biostudies-literature
| S-EPMC2765562 | biostudies-literature
| S-EPMC3332060 | biostudies-literature
| S-EPMC3499409 | biostudies-literature
| S-EPMC7816628 | biostudies-literature