Component
Rat thioredoxin 1 / Txn1
Rat thioredoxin 1 / Txn1
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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What it acts on
Adding 2.8 µM rat liver thioredoxin lowered apparent DHA Km of the thioredoxin-reductase system from 2.5 to 0.7 mM without materially increasing turnover.
Experimental context and source evidence
- cross_nutrient
- true
- experimental_model
- Purified rat liver thioredoxin reductase/thioredoxin and selenium-deficient rat liver
- exposure
- 2.8 µM thioredoxin added to NADPH/thioredoxin-reductase assay
- limitations
- Apparent kinetic effect is not proof of a faster whole-body recycling rate.
- nutrient_topic
- Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
- organism
- Rattus norvegicus
- plain_language
- Thioredoxin improved the system’s apparent affinity for oxidized vitamin C in this assay.
- primary_references
- [may1997] Reduction of dehydroascorbate to ascorbate by the selenoenzyme thioredoxin reductase. (1997). https://pubmed.ncbi.nlm.nih.gov/9278416/ DOI: 10.1074/jbc.272.36.22607
- tissue_or_cell_type
- Purified liver enzymes
Vitamin C: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 390–401
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified rat liver thioredoxin reductase/thioredoxin and selenium-deficient rat liver · source_derived_draft · unverified_draft
### vc-transport-thioredoxin-dha-affinity Adding 2.8 µM rat liver thioredoxin lowered apparent DHA Km of the thioredoxin-reductase system from 2.5 to 0.7 mM without materially increasing turnover. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: Thioredoxin improved the system’s apparent affinity for oxidized vitamin C in this assay. organism: Rattus norvegicus tissue_or_cell_type: Purified liver enzymes experimental_model: Purified rat liver thioredoxin reductase/thioredoxin and selenium-deficient rat liver limitations: Apparent kinetic effect is not proof of a faster whole-body recycling rate. exposure: 2.8 µM thioredoxin added to NADPH/thioredoxin-reductase assay cross_nutrient: true [may1997] Reduction of dehydroascorbate to ascorbate by the selenoenzyme thioredoxin reductase. (1997). https://pubmed.ncbi.nlm.nih.gov/9278416/ DOI: 10.1074/jbc.272.36.22607
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.