Component

Sodium occlusion by sodium-potassium ATPase

Sodium temporarily enclosed in the pump, inaccessible to surrounding solvent.

1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What acts on it

  1. Free Mg reduced apparent sodium affinity in pig-kidney pump sodium-22 occlusion experiments.

    Mg2+ → Sodium occlusion by sodium-potassium ATPase source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    Magnesium-dependent ATP chemistry is coupled to sodium and potassium handling by the pump; serum magnesium is not the enzyme-site concentration.
    experimental_model
    Partially purified pig-kidney pump; sodium-22 occlusion, EGCg quench-flow, ATP/Mg manipulations.
    limitations
    Equilibrium and Na-ATPase conditions; full Na/K exchange and systemic Mg deficiency were not tested.
    nutrient_topic
    Magnesium research collection; topical membership is not evidence of a direct dietary effect. · Magnesium
    organism
    Sus scrofa
    plain_language
    Magnesium can oppose sodium binding as well as support ATP chemistry.
    primary_references
    [faraj-2023-nka] Measurements of Na+-occluded intermediates during the catalytic cycle of the Na+/K+-ATPase provide novel insights into the mechanism of Na+ transport (2023). https://pmc.ncbi.nlm.nih.gov/articles/PMC9860123/ DOI: 10.1016/j.jbc.2022.102811
    tissue_or_cell_type
    Kidney enzyme membrane preparation

    Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 857–867

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Partially purified pig-kidney pump; sodium-22 occlusion, EGCg quench-flow, ATP/Mg manipulations. · source_derived_draft · unverified_draft

    ### mg-nka-free-mg-sodium-occlusion Free Mg reduced apparent sodium affinity in pig-kidney pump sodium-22 occlusion experiments. Condition category: normal nutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Magnesium can oppose sodium binding as well as support ATP chemistry. organism: Sus scrofa tissue_or_cell_type: Kidney enzyme membrane preparation experimental_model: Partially purified pig-kidney pump; sodium-22 occlusion, EGCg quench-flow, ATP/Mg manipulations. limitations: Equilibrium and Na-ATPase conditions; full Na/K exchange and systemic Mg deficiency were not tested. cross_nutrient: Magnesium-dependent ATP chemistry is coupled to sodium and potassium handling by the pump; serum magnesium is not the enzyme-site concentration. [faraj-2023-nka] Measurements of Na+-occluded intermediates during the catalytic cycle of the Na+/K+-ATPase provide novel insights into the mechanism of Na+ transport (2023). https://pmc.ncbi.nlm.nih.gov/articles/PMC9860123/ DOI: 10.1016/j.jbc.2022.102811
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards