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  • Title: Sulfhydryl group modification of photoreceptor G-protein prevents its light-induced binding to rhodopsin.
    Author: Reichert J, Hofmann KP.
    Journal: FEBS Lett; 1984 Mar 12; 168(1):121-4. PubMed ID: 6705917.
    Abstract:
    The effect of sulfhydryl modification on the light-induced interaction between rhodopsin and the peripheral GTP-binding protein of the photoreceptor membrane (G-protein) has been investigated by time-resolved near-infrared light-scattering and polyacrylamide gel electrophoresis. It has been found that the modification of rhodopsin with the alkylating agent N-ethylmaleimide (NEM) does not affect its light-induced interaction with the G-protein. Modification of G-protein with NEM or other sulfhydryl agents prevents any light-induced binding to rhodopsin. Dark-association of G to the membrane as well as the light-induced complex with rhodopsin (once formed) is insensitive to NEM.
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