Characterization of detergent-solubilized sarcoplasmic reticulum calcium ATPase by high-performance liquid chromatography
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00369a015
Reference41 articles.
1. The role of Mg2+ and Ca2+ in the simultaneous binding of vanadate and ATP at the phosphorylation site of sarcoplasmic reticulum Ca2+-ATPase
2. Equilibrium between monomers and oligomers of soluble Ca2+ -ATPase during the functional cycle
3. Properties of detergent-solubilized and membranous (Ca2+ + Mg2+)-activated ATPase from sarcoplasmic reticulum as studied by sulfhydryl reactivity and ESR spectroscopy
4. Immobilization of a spin-labeled fatty acid chain covalently attached to calcium(2+)-ATPase from sarcoplasmic reticulum suggests an oligomeric structure
5. The functional unit of sarcoplasmic reticulum Ca2+-ATPase. Active site titration and fluorescence measurements.
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