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Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments.
Wilden U, Hall SW, Kühn H. Wilden U, et al. Among authors: kuhn h. Proc Natl Acad Sci U S A. 1986 Mar;83(5):1174-8. doi: 10.1073/pnas.83.5.1174. Proc Natl Acad Sci U S A. 1986. PMID: 3006038 Free PMC article.
We report here that deactivation of PDEase in rod outer segment suspensions is highly enhanced by addition of ATP and purified 48-kDa protein, which is an intrinsic rod outer segment protein that is soluble in the dark but binds to photolyzed rhodopsin that has been phosphorylate …
We report here that deactivation of PDEase in rod outer segment suspensions is highly enhanced by addition of ATP and purified 48-kDa protei …
1,335 results