Duration and amplitude of the light-induced cGMP hydrolysis in vertebrate photoreceptors are regulated by multiple phosphorylation of rhodopsin and by arrestin binding.

@article{Wilden1995DurationAA,
  title={Duration and amplitude of the light-induced cGMP hydrolysis in vertebrate photoreceptors are regulated by multiple phosphorylation of rhodopsin and by arrestin binding.},
  author={Ursula Wilden},
  journal={Biochemistry},
  year={1995},
  volume={34 4},
  pages={1446-54}
}
The duration and amplitude of the light-induced cGMP hydrolysis in bovine rod outer segments were investigated using purified rhodopsin in nine different states of phosphorylation in a reconstituted system. Effects of varying amounts of arrestin at all states of rhodopsin phosphorylation were measured. The findings were the following: (1) At low bleaching levels, the activity of phosphodigesterase (PDE) depends strongly on the phosphorylation degree of the light-activated rhodopsin (R*), while… CONTINUE READING

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