Abstract
PHOSPHORYLATION of rhodopsin has been studied so far only in vitro. When suspensions of isolated and purified rod outer segments (ROS) from cattle and frogs have been mixed with γ–32P–ATP and Mg2+, upon illumination 32P–phosphate has been found to be bound covalently to rhodopsin in a slow dark reaction after bleaching. The activity of the water-extractable kinase which mediates the phosphate transfer was found to be independent of light, but rhodopsin was not acceptable as a substrate until it had been bleached by light4. The slow rate at which phosphorylation occurs (half time 3–5 min (refs 1–4)) suggests that it may be involved in light adaptation of the rods which also seems to be a slow process5.
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KÜHN, H. Light-dependent phosphorylation of rhodopsin in living frogs. Nature 250, 588–590 (1974). https://doi.org/10.1038/250588a0
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DOI: https://doi.org/10.1038/250588a0
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