The functional unit of sarcoplasmic reticulum Ca2+-ATPase. Active site titration and fluorescence measurements.

@article{Andersen1982TheFU,
  title={The functional unit of sarcoplasmic reticulum Ca2+-ATPase. Active site titration and fluorescence measurements.},
  author={Jens P Andersen and Jesper Vuust M\oller and Peter Leth J\orgensen},
  journal={The Journal of biological chemistry},
  year={1982},
  volume={257 14},
  pages={8300-7}
}
The properties of sarcoplasmic reticulum Ca2+-ATPase have been studied after modification of the ATP high affinity binding site with fluorescein isothiocyanate, both in the membranous state and after solubilization with the nonionic detergent, octaethyleneglycol monododecyl ether. Total inactivation of both membrane-bound and solubilized Ca2+-ATPase requires covalent attachment of 1 mol of fluorescein/mol of enzyme (115,000 g of protein) or per binding site for ATP. Sedimentation velocity… CONTINUE READING
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