Detailed characterization of the cooperative mechanism of Ca(2+) binding and catalytic activation in the Ca(2+) transport (SERCA) ATPase.

@article{Zhang2000DetailedCO,
  title={Detailed characterization of the cooperative mechanism of Ca(2+) binding and catalytic activation in the Ca(2+) transport (SERCA) ATPase.},
  author={Zhong Rong Zhang and David T. Lewis and Christopher L Strock and Giuseppe Inesi and Masayoshi Nakasako and Hiromi Nomura and Chikashi Toyoshima},
  journal={Biochemistry},
  year={2000},
  volume={39 30},
  pages={8758-67}
}
Expression of heterologous SERCA1a ATPase in Cos-1 cells was optimized to yield levels that account for 10-15% of the microsomal protein, as revealed by protein staining on electrophoretic gels. This high level of expression significantly improved our characterization of mutants, including direct measurements of Ca(2+) binding by the ATPase in the absence of ATP, and measurements of various enzyme functions in the presence of ATP or P(i). Mutational analysis distinguished two groups of amino… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 27 extracted citations

Membrane Proteins Production for Structural Analysis

Springer New York • 2014
View 3 Excerpts
Highly Influenced

Single-molecule analysis of phospholipid scrambling by TMEM16F

Proceedings of the National Academy of Sciences of the United States of America • 2018

Similar Papers

Loading similar papers…