Purification and characterization of the Mg2+-ATPase from rabbit skeletal muscle transverse tubule.

@article{Kirley1988PurificationAC,
  title={Purification and characterization of the Mg2+-ATPase from rabbit skeletal muscle transverse tubule.},
  author={Terence L. Kirley},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 25},
  pages={12682-9}
}
Transverse tubule membranes isolated from rabbit fast skeletal muscle contain a very active Mg2+-ATPase (ATP phosphohydrolase, EC 3.6.1.3). This enzyme is very sensitive to inactivation by most detergents. However, after solubilization with either lysolecithin or digitonin, the Mg2+-ATPase can be purified in active form. Using a combination of selective solubilization followed by lectin affinity chromatography, ion-exchange chromatography, and native gel electrophoresis, the Mg2+-ATPase has… CONTINUE READING

Citations

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

Similar Papers

Loading similar papers…