Coexistence of high- and low-affinity calcium binding sites of the sarcoplasmic reticulum calcium pump
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00089a025
Reference30 articles.
1. Sequential reactions in Pi utilization for ATP synthesis by sarcoplasmic reticulum.
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4. Acetyl Phosphate as Substrate for Ca2+ Uptake in Skeletal Muscle Microsomes
5. Energy Interconversion by the Ca2+-Dependent ATPase of the Sarcoplasmic Reticulum
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1. Ca2+ binding to sarcoplasmic reticulum ATPase phosphorylated by Pi reveals four thapsigargin-sensitive Ca2+ sites in the presence of ADP;Biochimica et Biophysica Acta (BBA) - Biomembranes;2004-12
2. Characterisation of thapsigargin-releasable Ca 2+ from the Ca 2+ -ATPase of sarcoplasmic reticulum at limiting [Ca 2+ ];Biochimica et Biophysica Acta (BBA) - Biomembranes;2000-12
3. Anionic phospholipids decrease the rate of slippage on the Ca2+-ATPase of sarcoplasmic reticulum;BIOCHEM J;1999
4. Luminal dissociation of Ca2+ from the phosphorylated Ca2+-ATPase is sequential and gated by Mg2+;BIOCHEM J;1999
5. Channelling free energy into work in biological processes;Experimental Physiology;1998-03-01
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