Component
Bovine protein disulfide isomerase / P4HB
Bovine protein disulfide isomerase / P4HB
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
Purified bovine liver protein disulfide isomerase catalyzed DHA reduction with GSH; apparent DHA Km was 1.0 mM.
Experimental context and source evidence
- cross_nutrient
- true
- experimental_model
- Purified human placental glutaredoxin and bovine liver PDI; additional porcine/bovine glutaredoxins
- exposure
- Purified PDI, DHA and GSH
- limitations
- Do not infer intact human endoplasmic-reticulum flux from this enzyme-capacity result.
- nutrient_topic
- Vitamin C research collection; topical membership is not evidence of a direct dietary effect. · Vitamin C
- organism
- Bos taurus
- plain_language
- A bovine protein-folding enzyme also recycled oxidized vitamin C in a purified assay.
- primary_references
- [wells1990] Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. (1990). https://pubmed.ncbi.nlm.nih.gov/2394726/ DOI: 10.1016/s0021-9258(18)55401-6
- tissue_or_cell_type
- Liver enzyme preparation
Vitamin C: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 364–375
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human placental glutaredoxin and bovine liver PDI; additional porcine/bovine glutaredoxins · source_derived_draft · unverified_draft
### vc-transport-bovine-pdi-dha Purified bovine liver protein disulfide isomerase catalyzed DHA reduction with GSH; apparent DHA Km was 1.0 mM. Condition category: normal nutrient_topic: Vitamin C research collection; topical membership is not evidence of a direct dietary effect. plain_language: A bovine protein-folding enzyme also recycled oxidized vitamin C in a purified assay. organism: Bos taurus tissue_or_cell_type: Liver enzyme preparation experimental_model: Purified human placental glutaredoxin and bovine liver PDI; additional porcine/bovine glutaredoxins limitations: Do not infer intact human endoplasmic-reticulum flux from this enzyme-capacity result. exposure: Purified PDI, DHA and GSH cross_nutrient: true [wells1990] Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. (1990). https://pubmed.ncbi.nlm.nih.gov/2394726/ DOI: 10.1016/s0021-9258(18)55401-6
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.