March 1, 1991Journal of Biological ChemistryOpen Access

Interaction of potassium and magnesium with the high affinity calcium-binding sites of the sarcoplasmic reticulum calcium-ATPase.

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Population

Sarcoplasmic reticulum Ca2(+)-ATPase of skeletal muscle

Design

Preclinical

Authors

MMMarie‐Jo MoutinCentre National de la Recherche Scientifique YDYves DupontSciensano (Belgium)

Discussion

Member takes

Implication

Should not yet inform clinical Ca2+ handling strategies; extends kinetic characterization of SERCA in animal models.

Structured PICO

Population

Sarcoplasmic reticulum Ca2(+)-ATPase of skeletal muscle

Intervention

Addition of Mg2+ and K+ ions

Outcome

Kinetics of intrinsic fluorescence changes produced by Ca2+ binding to and dissociation from the Ca2(+)-ATPasesurrogate

Mg2+ and K+ participate in specific steps of the Ca2+-binding mechanism of the sarcoplasmic reticulum Ca2+-ATPase, which may also serve as a pathway for monovalent ion fluxes in the absence of Ca2+.

Cite This Study

Moutin et al. (1991) studied this question.

synapsesocial.com/papers/6a894488b1e5d05ea8ec6686 https://doi.org/10.1016/s0021-9258(19)67634-9

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Interaction of potassium and magnesium with the high affinity calcium-binding sites of the sarcoplasmic reticulum calcium-ATPase.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Interaction of potassium and magnesium with the high affinity calcium-binding sites of the sarcoplasmic reticulum calcium-ATPase.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider