Activation of the erythrocyte Ca2+-ATPase by either self-association or interaction with calmodulin.

@article{KoskKosicka1988ActivationOT,
  title={Activation of the erythrocyte Ca2+-ATPase by either self-association or interaction with calmodulin.},
  author={Danuta Kosk-Kosicka and Tomasz Bzdega},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 34},
  pages={18184-9}
}
The octaethyleneglycol mono-n-dodecyl ether solubilized Ca2+-ATPase purified from human erythrocytes has been studied to determine the physical mechanism of its activation by calmodulin. The dependence of Ca2+-ATPase activity on the enzyme concentration shows a transformation from a calmodulin-dependent to a fully active calmodulin-independent form. The transformation is cooperative with a half-maximal activation at 10-20 nM enzyme. This suggests that at higher enzyme concentrations… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 24 extracted citations

Similar Papers

Loading similar papers…