Component

Bovine xanthine oxidoreductase / XDH

Context-specific entity; species, compartment and exposure are stated on each claim.

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

Read recorded mechanisms Open recursive mind map

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. Luteolin competitively inhibited purified bovine xanthine oxidase without time-dependent inhibition.

    Luteolin / 3′,4′,5,7-tetrahydroxyflavone → Bovine xanthine oxidoreductase / XDH source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Purified bovine enzyme steady-state kinetics.
    limitations
    Bovine enzyme evidence; not a clinical urate-lowering trial.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    It interfered with the purine-breakdown enzyme.
    primary_references
    Inhibition studies of bovine xanthine oxidase by luteolin, silibinin, quercetin, and curcumin. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19388706/ · DOI 10.1021/np8007123

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 284–290

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Purified bovine enzyme steady-state kinetics. · source_derived_draft · unverified_draft

    ## luteolin-xo-inhibition It interfered with the purine-breakdown enzyme. Luteolin competitively inhibited purified bovine xanthine oxidase without time-dependent inhibition. Model: Purified bovine enzyme steady-state kinetics. Limitations: Bovine enzyme evidence; not a clinical urate-lowering trial. Evidence access: Primary abstract Inhibition studies of bovine xanthine oxidase by luteolin, silibinin, quercetin, and curcumin. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19388706/ · DOI 10.1021/np8007123
    Complete structured claim and evidence

  2. Myricetin aglycone inhibited bovine-milk xanthine oxidase-mediated 6-mercaptopurine oxidation.

    Myricetin → Bovine xanthine oxidoreductase / XDH source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and repository full-text methods
    experimental_model
    Purified bovine-milk enzyme, chromatographic product analysis.
    limitations
    Sulfate was more potent than parent in the study. Not demonstrated human urate lowering or thiopurine toxicity.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    One enzyme processes both a natural purine and a medication.
    primary_references
    Inhibition of xanthine oxidase-catalyzed xanthine and 6-mercaptopurine oxidation by luteolin, naringenin, myricetin, ampelopsin and their conjugated metabolites. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37734263/ · DOI 10.1016/j.biopha.2023.115548

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 396–402

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified bovine-milk enzyme, chromatographic product analysis. · source_derived_draft · unverified_draft

    ## myricetin-xo-parent-6-mercaptopurine One enzyme processes both a natural purine and a medication. Myricetin aglycone inhibited bovine-milk xanthine oxidase-mediated 6-mercaptopurine oxidation. Model: Purified bovine-milk enzyme, chromatographic product analysis. Limitations: Sulfate was more potent than parent in the study. Not demonstrated human urate lowering or thiopurine toxicity. Evidence access: Primary abstract and repository full-text methods Inhibition of xanthine oxidase-catalyzed xanthine and 6-mercaptopurine oxidation by luteolin, naringenin, myricetin, ampelopsin and their conjugated metabolites. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37734263/ · DOI 10.1016/j.biopha.2023.115548
    Complete structured claim and evidence

  3. Myricetin aglycone inhibited bovine-milk xanthine oxidase-mediated xanthine oxidation.

    Myricetin → Bovine xanthine oxidoreductase / XDH source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and repository full-text methods
    experimental_model
    Purified bovine-milk enzyme, chromatographic product analysis.
    limitations
    Sulfate was more potent than parent in the study. Not demonstrated human urate lowering or thiopurine toxicity.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    One enzyme processes both a natural purine and a medication.
    primary_references
    Inhibition of xanthine oxidase-catalyzed xanthine and 6-mercaptopurine oxidation by luteolin, naringenin, myricetin, ampelopsin and their conjugated metabolites. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37734263/ · DOI 10.1016/j.biopha.2023.115548

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 388–394

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified bovine-milk enzyme, chromatographic product analysis. · source_derived_draft · unverified_draft

    ## myricetin-xo-parent-xanthine One enzyme processes both a natural purine and a medication. Myricetin aglycone inhibited bovine-milk xanthine oxidase-mediated xanthine oxidation. Model: Purified bovine-milk enzyme, chromatographic product analysis. Limitations: Sulfate was more potent than parent in the study. Not demonstrated human urate lowering or thiopurine toxicity. Evidence access: Primary abstract and repository full-text methods Inhibition of xanthine oxidase-catalyzed xanthine and 6-mercaptopurine oxidation by luteolin, naringenin, myricetin, ampelopsin and their conjugated metabolites. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37734263/ · DOI 10.1016/j.biopha.2023.115548
    Complete structured claim and evidence

  4. Myricetin 3′-O-sulfate inhibited bovine-milk xanthine oxidase-mediated 6-mercaptopurine oxidation.

    Myricetin 3′-O-sulfate → Bovine xanthine oxidoreductase / XDH source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and repository full-text methods
    experimental_model
    Purified bovine-milk enzyme, chromatographic product analysis.
    limitations
    Sulfate was more potent than parent in the study. Not demonstrated human urate lowering or thiopurine toxicity.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    One enzyme processes both a natural purine and a medication.
    primary_references
    Inhibition of xanthine oxidase-catalyzed xanthine and 6-mercaptopurine oxidation by luteolin, naringenin, myricetin, ampelopsin and their conjugated metabolites. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37734263/ · DOI 10.1016/j.biopha.2023.115548

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 412–418

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified bovine-milk enzyme, chromatographic product analysis. · source_derived_draft · unverified_draft

    ## myricetin-xo-sulfate-6-mercaptopurine One enzyme processes both a natural purine and a medication. Myricetin 3′-O-sulfate inhibited bovine-milk xanthine oxidase-mediated 6-mercaptopurine oxidation. Model: Purified bovine-milk enzyme, chromatographic product analysis. Limitations: Sulfate was more potent than parent in the study. Not demonstrated human urate lowering or thiopurine toxicity. Evidence access: Primary abstract and repository full-text methods Inhibition of xanthine oxidase-catalyzed xanthine and 6-mercaptopurine oxidation by luteolin, naringenin, myricetin, ampelopsin and their conjugated metabolites. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37734263/ · DOI 10.1016/j.biopha.2023.115548
    Complete structured claim and evidence

  5. Myricetin 3′-O-sulfate inhibited bovine-milk xanthine oxidase-mediated xanthine oxidation.

    Myricetin 3′-O-sulfate → Bovine xanthine oxidoreductase / XDH source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and repository full-text methods
    experimental_model
    Purified bovine-milk enzyme, chromatographic product analysis.
    limitations
    Sulfate was more potent than parent in the study. Not demonstrated human urate lowering or thiopurine toxicity.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    One enzyme processes both a natural purine and a medication.
    primary_references
    Inhibition of xanthine oxidase-catalyzed xanthine and 6-mercaptopurine oxidation by luteolin, naringenin, myricetin, ampelopsin and their conjugated metabolites. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37734263/ · DOI 10.1016/j.biopha.2023.115548

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 404–410

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified bovine-milk enzyme, chromatographic product analysis. · source_derived_draft · unverified_draft

    ## myricetin-xo-sulfate-xanthine One enzyme processes both a natural purine and a medication. Myricetin 3′-O-sulfate inhibited bovine-milk xanthine oxidase-mediated xanthine oxidation. Model: Purified bovine-milk enzyme, chromatographic product analysis. Limitations: Sulfate was more potent than parent in the study. Not demonstrated human urate lowering or thiopurine toxicity. Evidence access: Primary abstract and repository full-text methods Inhibition of xanthine oxidase-catalyzed xanthine and 6-mercaptopurine oxidation by luteolin, naringenin, myricetin, ampelopsin and their conjugated metabolites. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37734263/ · DOI 10.1016/j.biopha.2023.115548
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Luteolin reduced superoxide production by purified bovine xanthine oxidase.

    Luteolin / 3′,4′,5,7-tetrahydroxyflavone → Superoxide radical anion source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Bovine enzyme assays.
    limitations
    Does not establish antioxidant benefit across tissues.
    nutrient_topic
    Luteolin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Luteolin / 3′,4′,5,7-tetrahydroxyflavone
    plain_language
    Blocking the enzyme also reduced its radical output.
    primary_references
    Inhibition studies of bovine xanthine oxidase by luteolin, silibinin, quercetin, and curcumin. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19388706/ · DOI 10.1021/np8007123

    Luteolin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 292–298

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Bovine enzyme assays. · source_derived_draft · unverified_draft

    ## luteolin-xo-superoxide Blocking the enzyme also reduced its radical output. Luteolin reduced superoxide production by purified bovine xanthine oxidase. Model: Bovine enzyme assays. Limitations: Does not establish antioxidant benefit across tissues. Evidence access: Primary abstract Inhibition studies of bovine xanthine oxidase by luteolin, silibinin, quercetin, and curcumin. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19388706/ · DOI 10.1021/np8007123
    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