[15] Synthesis of atp from Ca2+ gradient by sarcoplasmic reticulum Ca2+ 
transport ATPase

Fassold, E.; Hasselbach, Wilhelm

doi:10.1016/0076-6879(88)57077-5

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[15] Synthesis of atp from Ca2+ gradient by sarcoplasmic reticulum Ca2+ transport ATPase

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Hasselbach, Wilhelm
Department of Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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https://www.sciencedirect.com/science/article/abs/pii/0076687988570775?via%3Dihub
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引用

Fassold, E., & Hasselbach, W. (1988). [15] Synthesis of atp from Ca2+ gradient by sarcoplasmic reticulum Ca2+ transport ATPase. In Methods in Enzymology (pp. 220-228). New York, NY [u.a.]: Elsevier.

引用: https://hdl.handle.net/21.11116/0000-000A-9FD0-8

要旨

This chapter focuses on the synthesis of ATP from Ca2+ gradient by sarcoplasmic reticulum Ca2+ transport ATPase. Sarcoplasmic reticulum vesicles isolated from rabbit skeletal muscle consist of tightly sealed membranes, which only allow a slow passive back-diffusion of Ca2+ taken up previously by a pathway not yet identified. The driving force for ATP formation is the Ca2+ gradient existing between the vesicular volume and the external medium. Conditions are chosen in such a way that nearly all Ca2+ that was released could contribute to ATP synthesis. Loading of the vesicles is usually performed in the presence of acetyl phosphate (AcP) as energy-yielding substrate, and inorganic phosphate (Pi) serving as precipitating anion and substrate for the backward reaction. Ca2+ loads obtained by slow passive diffusion of millimolar concentrations (<100 nmol/mg protein) or by active transport in the absence of a precipitating anion (100–200 nmol/mg protein) set limits to the duration of the two fast-occurring processes, and to the accuracy of the results obtained.