Characterization and photoaffinity labeling of the ATP binding site of the ryanodine receptor from skeletal muscle.

@article{Zarka1993CharacterizationAP,
  title={Characterization and photoaffinity labeling of the ATP binding site of the ryanodine receptor from skeletal muscle.},
  author={Aliza Zarka and Varda Shoshan-Barmatz},
  journal={European journal of biochemistry},
  year={1993},
  volume={213 1},
  pages={147-54}
}
The photoaffinity analog of ATP, 3'-O-(4-benzoyl)benzoyl-adenosine 5'-triphosphate (Bz2ATP) was used to covalently label and to identify the ATP binding site of the skeletal muscle ryanodine receptor. Like ATP, Bz2ATP stimulates up to fivefold the binding of ryanodine to its receptor. Photoactivation by ultraviolet light of the benzophenone group in the [alpha-32P]Bz2ATP results in covalent binding of [alpha-32P]Bz2ATP to the 450-kDa polypeptide, the ryanodine receptor's subunit. An apparent… CONTINUE READING
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