English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Charge translocation by the sarcoplasmic Ca ATPase after an ATP concentration jump

MPS-Authors
/persons/resource/persons137696

Hartung,  Klaus
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137653

Fendler,  Klaus
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Hartung, K., & Fendler, K. (1989). Charge translocation by the sarcoplasmic Ca ATPase after an ATP concentration jump. Journal of Protein Chemistry, 8(3), 377-379. doi:10.1007/BF01674287.


Cite as: http://hdl.handle.net/21.11116/0000-0007-1FCE-0
Abstract
The Ca ATPase of the sarcoplasmic reticulum (SR) translocates Ca from the cytoplasmic space into the lumen of the SR using ATP hydrolysis as an energy source. The established stochiometry is 2 Ca/ATP (Hasselbach, 1978). The electrical current related to the turnover of this transport enzyme could be measured recently (Hartung et al., 1987) by adopting a method introduced for the measurement of pump currents generated by the NaK ATPase (Fendler et al., 1985). Vesicles derived from fragmented SR are adsorbed on one side of a planar (black) lipid membrane, acting as a capacitive electrode. Ca transport by the Ca ATPase is initiated by an ATP concentration jump which is achieved by the photolysis of caged ATP (Kaplan et al., 1978).