Component
Human haptocorrin / TCN1
Human haptocorrin / TCN1
7 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
In egg-yolk transfer assays, human R binder accepted released cobalamin, whereas direct transfer to intrinsic factor was not detected and R-binder-deficient gastric juice failed to accept it.
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice
- exposure
- Acidified human saliva/gastric juice with egg-yolk-bound radiocobalamin
- limitations
- Food-specific biochemical model; this pH threshold is not a clinical blood threshold or proof that all foods behave identically. Pepsin preparation species was not specified in the inspected abstract.
- nutrient_topic
- Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
- organism
- Homo sapiens
- plain_language
- The first observed carrier was haptocorrin.
- primary_references
- [carmel-1990-food-transfer] Transfer of cobalamin from the cobalamin-binding protein of egg yolk to R binder of human saliva and gastric juice. (1990). https://pubmed.ncbi.nlm.nih.gov/2110915/ DOI: 10.1016/0016-5085(90)91076-i
- tissue_or_cell_type
- Gastric luminal digestion model
Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 114–125
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice · source_derived_draft · unverified_draft
### b12-abs-food-haptocorrin-capture In egg-yolk transfer assays, human R binder accepted released cobalamin, whereas direct transfer to intrinsic factor was not detected and R-binder-deficient gastric juice failed to accept it. Condition category: normal nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: The first observed carrier was haptocorrin. organism: Homo sapiens tissue_or_cell_type: Gastric luminal digestion model experimental_model: In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice limitations: Food-specific biochemical model; this pH threshold is not a clinical blood threshold or proof that all foods behave identically. Pepsin preparation species was not specified in the inspected abstract. exposure: Acidified human saliva/gastric juice with egg-yolk-bound radiocobalamin cross_nutrient: false [carmel-1990-food-transfer] Transfer of cobalamin from the cobalamin-binding protein of egg yolk to R binder of human saliva and gastric juice. (1990). https://pubmed.ncbi.nlm.nih.gov/2110915/ DOI: 10.1016/0016-5085(90)91076-i
Complete structured claim and evidenceHuman salivary R protein bound cobalamin with 50-fold higher affinity than human intrinsic factor at pH 2 and threefold higher affinity at pH 8.
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- Purified human salivary R protein and gastric intrinsic factor in vitro
- exposure
- pH 2 or 8; purified protein competition
- limitations
- Reconstituted binding/protease conditions; measured competition does not quantify absorption in an intact person. Individual protease isoforms and reagent species not resolved in abstract.
- nutrient_topic
- Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
- organism
- Homo sapiens
- plain_language
- Haptocorrin outcompeted intrinsic factor, especially in acid.
- primary_references
- [allen-1978-proteases] Effect of proteolytic enzymes on the binding of cobalamin to R protein and intrinsic factor. In vitro evidence that a failure to partially degrade R protein is responsible for cobalamin malabsorption in pancreatic insufficiency. (1978). https://pubmed.ncbi.nlm.nih.gov/22556/ DOI: 10.1172/jci108924
- tissue_or_cell_type
- Salivary/gastric and intestinal luminal binding models
Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 153–164
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human salivary R protein and gastric intrinsic factor in vitro · source_derived_draft · unverified_draft
### b12-abs-haptocorrin-affinity Human salivary R protein bound cobalamin with 50-fold higher affinity than human intrinsic factor at pH 2 and threefold higher affinity at pH 8. Condition category: normal nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Haptocorrin outcompeted intrinsic factor, especially in acid. organism: Homo sapiens tissue_or_cell_type: Salivary/gastric and intestinal luminal binding models experimental_model: Purified human salivary R protein and gastric intrinsic factor in vitro limitations: Reconstituted binding/protease conditions; measured competition does not quantify absorption in an intact person. Individual protease isoforms and reagent species not resolved in abstract. exposure: pH 2 or 8; purified protein competition cross_nutrient: false [allen-1978-proteases] Effect of proteolytic enzymes on the binding of cobalamin to R protein and intrinsic factor. In vitro evidence that a failure to partially degrade R protein is responsible for cobalamin malabsorption in pancreatic insufficiency. (1978). https://pubmed.ncbi.nlm.nih.gov/22556/ DOI: 10.1172/jci108924
Complete structured claim and evidence
Where it participates (unsigned role)
In the egg-yolk/human saliva model, acidification to pH 1.5 permitted limited cobalamin transfer to R binder; virtually none occurred above pH 2 despite pepsin.
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice
- exposure
- In vitro pH manipulation
- limitations
- Food-specific biochemical model; this pH threshold is not a clinical blood threshold or proof that all foods behave identically. Pepsin preparation species was not specified in the inspected abstract.
- nutrient_topic
- Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
- organism
- Homo sapiens
- plain_language
- Acid enabled release and capture of B12 from this food model.
- primary_references
- [carmel-1990-food-transfer] Transfer of cobalamin from the cobalamin-binding protein of egg yolk to R binder of human saliva and gastric juice. (1990). https://pubmed.ncbi.nlm.nih.gov/2110915/ DOI: 10.1016/0016-5085(90)91076-i
- tissue_or_cell_type
- Gastric luminal digestion model
Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 88–99
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice · source_derived_draft · unverified_draft
### b12-abs-food-acid In the egg-yolk/human saliva model, acidification to pH 1.5 permitted limited cobalamin transfer to R binder; virtually none occurred above pH 2 despite pepsin. Condition category: normal nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Acid enabled release and capture of B12 from this food model. organism: Homo sapiens tissue_or_cell_type: Gastric luminal digestion model experimental_model: In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice limitations: Food-specific biochemical model; this pH threshold is not a clinical blood threshold or proof that all foods behave identically. Pepsin preparation species was not specified in the inspected abstract. exposure: In vitro pH manipulation cross_nutrient: false [carmel-1990-food-transfer] Transfer of cobalamin from the cobalamin-binding protein of egg yolk to R binder of human saliva and gastric juice. (1990). https://pubmed.ncbi.nlm.nih.gov/2110915/ DOI: 10.1016/0016-5085(90)91076-i
Complete structured claim and evidenceAdding pepsin at 1,200 U/mL under acidic conditions increased egg-yolk cobalamin transfer to human salivary or gastric R binders to 39-58%.
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice
- exposure
- Pepsin supplementation at acidic pH
- limitations
- Food-specific biochemical model; this pH threshold is not a clinical blood threshold or proof that all foods behave identically. Pepsin preparation species was not specified in the inspected abstract.
- nutrient_topic
- Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
- organism
- Homo sapiens
- plain_language
- Pepsin helped haptocorrin capture food-bound B12.
- primary_references
- [carmel-1990-food-transfer] Transfer of cobalamin from the cobalamin-binding protein of egg yolk to R binder of human saliva and gastric juice. (1990). https://pubmed.ncbi.nlm.nih.gov/2110915/ DOI: 10.1016/0016-5085(90)91076-i
- tissue_or_cell_type
- Gastric luminal digestion model
Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 101–112
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice · source_derived_draft · unverified_draft
### b12-abs-food-pepsin Adding pepsin at 1,200 U/mL under acidic conditions increased egg-yolk cobalamin transfer to human salivary or gastric R binders to 39-58%. Condition category: normal nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Pepsin helped haptocorrin capture food-bound B12. organism: Homo sapiens tissue_or_cell_type: Gastric luminal digestion model experimental_model: In vitro egg-yolk cobalamin-binding protein mixed with human saliva/gastric juice limitations: Food-specific biochemical model; this pH threshold is not a clinical blood threshold or proof that all foods behave identically. Pepsin preparation species was not specified in the inspected abstract. exposure: Pepsin supplementation at acidic pH cross_nutrient: false [carmel-1990-food-transfer] Transfer of cobalamin from the cobalamin-binding protein of egg yolk to R binder of human saliva and gastric juice. (1990). https://pubmed.ncbi.nlm.nih.gov/2110915/ DOI: 10.1016/0016-5085(90)91076-i
Complete structured claim and evidenceIn three patients with pancreatic insufficiency, oral cobinamide 100 nmol corrected malabsorption of 0.4 nmol radiocobalamin in Schilling tests, comparably to trypsin.
Experimental context and source evidence
- availability_state
- machinery_impairment Imported condition classification; unverified.
- cross_nutrient
- false
- experimental_model
- Three human pancreatic-insufficiency patients and parallel human binding assays
- exposure
- Cobinamide competitor during Schilling test
- limitations
- Small physiological intervention; cobinamide is an experimental analogue, not B12 nutrition. The absorption defect was pancreatic machinery impairment.
- nutrient_topic
- Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
- organism
- Homo sapiens
- plain_language
- Blocking haptocorrin competition restored tracer absorption in three patients.
- primary_references
- [allen-1978-cobinamide] Correction of cobalamin malabsorption in pancreatic insufficiency with a cobalamin analogue that binds with high affinity to R protein but not to intrinsic factor. In vivo evidence that a failure to partially degrade R protein is responsible for cobalamin malabsorption in pancreatic insufficiency. (1978). https://pubmed.ncbi.nlm.nih.gov/659618/ DOI: 10.1172/jci109083
- tissue_or_cell_type
- Intestinal absorption and urinary radiotracer recovery
- trigger_kind
- machinery_impairment Imported condition classification; unverified.
Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 205–216
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Three human pancreatic-insufficiency patients and parallel human binding assays · source_derived_draft · unverified_draft
### b12-abs-pancreatic-competitor-rescue In three patients with pancreatic insufficiency, oral cobinamide 100 nmol corrected malabsorption of 0.4 nmol radiocobalamin in Schilling tests, comparably to trypsin. Condition category: machinery_impairment nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Blocking haptocorrin competition restored tracer absorption in three patients. organism: Homo sapiens tissue_or_cell_type: Intestinal absorption and urinary radiotracer recovery experimental_model: Three human pancreatic-insufficiency patients and parallel human binding assays limitations: Small physiological intervention; cobinamide is an experimental analogue, not B12 nutrition. The absorption defect was pancreatic machinery impairment. exposure: Cobinamide competitor during Schilling test cross_nutrient: false [allen-1978-cobinamide] Correction of cobalamin malabsorption in pancreatic insufficiency with a cobalamin analogue that binds with high affinity to R protein but not to intrinsic factor. In vivo evidence that a failure to partially degrade R protein is responsible for cobalamin malabsorption in pancreatic insufficiency. (1978). https://pubmed.ncbi.nlm.nih.gov/659618/ DOI: 10.1172/jci109083
Complete structured claim and evidencePancreatic protease incubation at pH 8 partially degraded human R protein and lowered its cobalamin affinity approximately 150-fold.
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- Purified human salivary R protein and gastric intrinsic factor in vitro
- exposure
- Pancreatic proteases at pH 8
- limitations
- Reconstituted binding/protease conditions; measured competition does not quantify absorption in an intact person. Individual protease isoforms and reagent species not resolved in abstract.
- nutrient_topic
- Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
- organism
- Homo sapiens
- plain_language
- Digestive proteases loosened haptocorrin binding.
- primary_references
- [allen-1978-proteases] Effect of proteolytic enzymes on the binding of cobalamin to R protein and intrinsic factor. In vitro evidence that a failure to partially degrade R protein is responsible for cobalamin malabsorption in pancreatic insufficiency. (1978). https://pubmed.ncbi.nlm.nih.gov/22556/ DOI: 10.1172/jci108924
- tissue_or_cell_type
- Duodenal luminal model
Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 166–177
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human salivary R protein and gastric intrinsic factor in vitro · source_derived_draft · unverified_draft
### b12-abs-proteolysis-affinity Pancreatic protease incubation at pH 8 partially degraded human R protein and lowered its cobalamin affinity approximately 150-fold. Condition category: normal nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Digestive proteases loosened haptocorrin binding. organism: Homo sapiens tissue_or_cell_type: Duodenal luminal model experimental_model: Purified human salivary R protein and gastric intrinsic factor in vitro limitations: Reconstituted binding/protease conditions; measured competition does not quantify absorption in an intact person. Individual protease isoforms and reagent species not resolved in abstract. exposure: Pancreatic proteases at pH 8 cross_nutrient: false [allen-1978-proteases] Effect of proteolytic enzymes on the binding of cobalamin to R protein and intrinsic factor. In vitro evidence that a failure to partially degrade R protein is responsible for cobalamin malabsorption in pancreatic insufficiency. (1978). https://pubmed.ncbi.nlm.nih.gov/22556/ DOI: 10.1172/jci108924
Complete structured claim and evidenceProtease treatment of R-protein-bound cobalamin enabled complete transfer to human intrinsic factor within ten minutes; without proteases, transfer was not observed at pH 2 or 8.
Experimental context and source evidence
- cross_nutrient
- false
- experimental_model
- Purified human salivary R protein and gastric intrinsic factor in vitro
- exposure
- R protein-Cbl plus pancreatic proteases and IF
- limitations
- Reconstituted binding/protease conditions; measured competition does not quantify absorption in an intact person. Individual protease isoforms and reagent species not resolved in abstract.
- nutrient_topic
- Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
- organism
- Homo sapiens
- plain_language
- Proteolysis enabled B12 to switch carriers.
- primary_references
- [allen-1978-proteases] Effect of proteolytic enzymes on the binding of cobalamin to R protein and intrinsic factor. In vitro evidence that a failure to partially degrade R protein is responsible for cobalamin malabsorption in pancreatic insufficiency. (1978). https://pubmed.ncbi.nlm.nih.gov/22556/ DOI: 10.1172/jci108924
- tissue_or_cell_type
- Duodenal luminal model
Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 179–190
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human salivary R protein and gastric intrinsic factor in vitro · source_derived_draft · unverified_draft
### b12-abs-proteolysis-transfer Protease treatment of R-protein-bound cobalamin enabled complete transfer to human intrinsic factor within ten minutes; without proteases, transfer was not observed at pH 2 or 8. Condition category: normal nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Proteolysis enabled B12 to switch carriers. organism: Homo sapiens tissue_or_cell_type: Duodenal luminal model experimental_model: Purified human salivary R protein and gastric intrinsic factor in vitro limitations: Reconstituted binding/protease conditions; measured competition does not quantify absorption in an intact person. Individual protease isoforms and reagent species not resolved in abstract. exposure: R protein-Cbl plus pancreatic proteases and IF cross_nutrient: false [allen-1978-proteases] Effect of proteolytic enzymes on the binding of cobalamin to R protein and intrinsic factor. In vitro evidence that a failure to partially degrade R protein is responsible for cobalamin malabsorption in pancreatic insufficiency. (1978). https://pubmed.ncbi.nlm.nih.gov/22556/ DOI: 10.1172/jci108924
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.