Conformational basis of the phospholipid requirement for the activity of SR Ca(2+)-ATPase.

@article{Zhang1998ConformationalBO,
  title={Conformational basis of the phospholipid requirement for the activity of SR Ca(2+)-ATPase.},
  author={Xiaoying Zhang and Xiaoshan Min and Fu-yu Yang},
  journal={Chemistry and physics of lipids},
  year={1998},
  volume={97 1},
  pages={55-64}
}
The delipidated sarcoplasmic reticulum (SR) Ca(2+)-ATPase was reconstituted into proteoliposomes containing different phospholipids. The result demonstrated the necessity of phosphatidylcholine (PC) for optimal ATPase activity and phosphatidylethanolamine (PE) for the optimal calcium transport activity. Fluorescence intensity of Fluorescein 5-isothiocyanate (FITC)-labeled enzyme at Lys515 as well as the measurement of the distance between 5-((2-[(iodoacetyl) amino] ethyl) amino)naphthalene-1… CONTINUE READING