Molecular, enzymatic and functional properties of rhodopsin kinase from rat pineal gland

@article{Palczewski1990MolecularEA,
  title={Molecular, enzymatic and functional properties of rhodopsin kinase from rat pineal gland},
  author={Krzysztof Palczewski and Michael E. Carruth and Grazyna Adamus and J. Hugh McDowell and Paul A. Hargrave},
  journal={Vision Research},
  year={1990},
  volume={30},
  pages={1129-1137}
}
Rhodopsin kinase activity from rat pineal gland and from rat retina are indistinguishable, based upon determination of a variety of enzymatic and molecular properties. Both activities are independent of calcium, cyclic nucleotides, and calmodulin. Both are activated by spermine and inhibited by adenosine and some rhodopsin kinase specific adenosine derivatives such as sangivamycin. The Km's for rhodopsin, ATP, and GTP are indistinguishable for the protein kinase in extracts from the retina and… CONTINUE READING
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