Component

Thermal stability of human CA2

Purified CA2 unfolding transition measured by differential scanning calorimetry.

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. Zinc-containing CA2 unfolded at 59±0.5°C versus 51±0.5°C for the chelated preparation in differential scanning calorimetry.

    Zinc(II) ion → Thermal stability of human CA2 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange
    exposure
    Purified apo and holo proteins; DSC in 50 mM Tris-HCl pH 7.0.
    limitations
    Purified recombinant protein; chelation is not dietary deficiency. Approximately 10% zinc remained in the nominal apo preparation. Thermal unfolding temperature is not a body-temperature requirement.
    nutrient_topic
    Zinc research collection; topical membership is not evidence of a direct dietary effect. · Zinc
    organism
    Homo sapiens
    plain_language
    Bound zinc also helps CA2 resist thermal unfolding.
    primary_references
    [zinc-enz-ca2-apo2009] Apo-human carbonic anhydrase II revisited: implications of the loss of a metal in protein structure, stability, and solvent network. (2009). https://pubmed.ncbi.nlm.nih.gov/19583303/ DOI: 10.1021/bi9007512
    tissue_or_cell_type
    Purified protein; cell-free assay

    Zinc: transport, enzyme loading, deficiency and nutrient interactions (2026-09-17) · lines 625–636

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange · source_derived_draft · unverified_draft

    ### zinc-enz-ca2-stability Zinc-containing CA2 unfolded at 59±0.5°C versus 51±0.5°C for the chelated preparation in differential scanning calorimetry. Condition category: normal nutrient_topic: Zinc research collection; topical membership is not evidence of a direct dietary effect. plain_language: Bound zinc also helps CA2 resist thermal unfolding. organism: Homo sapiens tissue_or_cell_type: Purified protein; cell-free assay experimental_model: Purified recombinant human CA2 expressed in E. coli; chelation, crystallography, DSC and H/D exchange limitations: Purified recombinant protein; chelation is not dietary deficiency. Approximately 10% zinc remained in the nominal apo preparation. Thermal unfolding temperature is not a body-temperature requirement. exposure: Purified apo and holo proteins; DSC in 50 mM Tris-HCl pH 7.0. cross_nutrient: false [zinc-enz-ca2-apo2009] Apo-human carbonic anhydrase II revisited: implications of the loss of a metal in protein structure, stability, and solvent network. (2009). https://pubmed.ncbi.nlm.nih.gov/19583303/ DOI: 10.1021/bi9007512
    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