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

Hartung, Klaus; Fendler, Klaus

doi:10.1007/BF01674287

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

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

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

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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: https://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).