Purification and properties of a vanadate- and N-ethylmaleimide-sensitive ATPase from chromaffin granule membranes.

@article{Moriyama1988PurificationAP,
  title={Purification and properties of a vanadate- and N-ethylmaleimide-sensitive ATPase from chromaffin granule membranes.},
  author={Yoshinori Moriyama and Nathan Alfred Nelson},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 17},
  pages={8521-7}
}
A vanadate- and N-ethylmaleimide-sensitive ATPase was purified about 500-fold from chromaffin granule membranes. The purified preparation contained a single major polypeptide with an apparent molecular mass of about 115 kDa, which was copurified with the ATPase activity. Immunological studies revealed that this polypeptide has no relation to subunit I (115 kDa) of the H+-ATPase from chromaffin granules. The ATPase activity of the enzyme is inhibited about 50% by 100 microM N-ethylmaleimide or 5… CONTINUE READING