Component

Bovine liver low-molecular-weight chromium-binding isolate / chromodulin candidate

Bovine liver low-molecular-weight chromium-binding isolate / chromodulin candidate. Species, exposure and limitations are retained in each linked claim.

5 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 it acts on

  1. The low-molecular-weight chromium-binding preparation bound insulin-activated rat insulin receptor with a reported dissociation constant near 250 pM.

    Bovine liver low-molecular-weight chromium-binding isolate / chromodulin candidate → Rat insulin receptor / Insr source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/chromium-research/9109644.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "23e955cef071c135f3935f440f4e333d49f494f004ceb22574df717c86bb7283", "start_char": 0, "end_char": 939, "text_sha256": "23e955cef071c135f3935f440f4e333d49f494f004ceb22574df717c86bb7283"}
    experimental_model
    Isolated rat insulin receptor and adipocyte membrane kinase assays
    exposure
    Insulin activation with added low-molecular-weight chromium-binding material
    limitations
    Assay activity is distinct from proof of an endogenous human cofactor. The peptide preparation and its cellular origin remain disputed; chromium is not shown to be an obligatory catalytic metal of INSR.
    nutrient_topic
    Chromium research collection; topical membership is not evidence of a direct dietary effect. · Chromium
    organism
    Rat receptor; isolated chromium oligopeptide preparation
    plain_language
    An isolated chromium-binding preparation attached to an activated rat insulin receptor in the assay.
    primary_references
    [chromium-p9109644] Chromium oligopeptide activates insulin receptor tyrosine kinase activity. (1997). https://pubmed.ncbi.nlm.nih.gov/9109644/ DOI: 10.1021/bi963154t
    tissue_or_cell_type
    Purified receptor and membrane fragments

    Chromium: transport, insulin signaling, nutrient interactions and essentiality debate (2026-09-17) · lines 250–261

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Isolated rat insulin receptor and adipocyte membrane kinase assays · source_derived_draft · unverified_draft

    ### chromium-chromodulin-insr-binding The low-molecular-weight chromium-binding preparation bound insulin-activated rat insulin receptor with a reported dissociation constant near 250 pM. Condition category: normal nutrient_topic: Chromium research collection; topical membership is not evidence of a direct dietary effect. plain_language: An isolated chromium-binding preparation attached to an activated rat insulin receptor in the assay. organism: Rat receptor; isolated chromium oligopeptide preparation tissue_or_cell_type: Purified receptor and membrane fragments experimental_model: Isolated rat insulin receptor and adipocyte membrane kinase assays limitations: Assay activity is distinct from proof of an endogenous human cofactor. The peptide preparation and its cellular origin remain disputed; chromium is not shown to be an obligatory catalytic metal of INSR. exposure: Insulin activation with added low-molecular-weight chromium-binding material evidence_span: {"source_cache": "artifacts/chromium-research/9109644.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "23e955cef071c135f3935f440f4e333d49f494f004ceb22574df717c86bb7283", "start_char": 0, "end_char": 939, "text_sha256": "23e955cef071c135f3935f440f4e333d49f494f004ceb22574df717c86bb7283"} [chromium-p9109644] Chromium oligopeptide activates insulin receptor tyrosine kinase activity. (1997). https://pubmed.ncbi.nlm.nih.gov/9109644/ DOI: 10.1021/bi963154t
    Complete structured claim and evidence

  2. The bovine-liver low-molecular-weight isolate contained approximately four Cr(III) ions per peptide, with spectra consistent with carboxylate-supported metal assemblies; one tetranuclear versus two dinuclear assemblies was unresolved.

    Bovine liver low-molecular-weight chromium-binding isolate / chromodulin candidate → Trivalent chromium / Cr(III) source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/chromium-research/9056266.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "36be61aa6271d3491a4432d31d5ea6524a059fcc1f1ba1e0acac5f175f711a06", "start_char": 0, "end_char": 791, "text_sha256": "36be61aa6271d3491a4432d31d5ea6524a059fcc1f1ba1e0acac5f175f711a06"}
    experimental_model
    Isolation and spectroscopy of a bovine-liver chromium-containing peptide fraction
    exposure
    Spectroscopic characterization of an isolate with approximately four Cr(III) ions per peptide
    limitations
    The paper interpreted the isolate as naturally occurring; later work questioned whether similar low-molecular-weight species arise during extraction. Exact nuclearity was not resolved by this study.
    nutrient_topic
    Chromium research collection; topical membership is not evidence of a direct dietary effect. · Chromium
    organism
    Bovine liver isolate
    plain_language
    Researchers isolated a chromium-binding peptide fraction, but its structure and origin inside living cells were not fully settled.
    primary_references
    [chromium-p9056266] Isolation and characterization of a biologically active chromium oligopeptide from bovine liver. (1997). https://pubmed.ncbi.nlm.nih.gov/9056266/ DOI: 10.1006/abbi.1997.9878
    tissue_or_cell_type
    Purified fraction outside intact cells

    Chromium: transport, insulin signaling, nutrient interactions and essentiality debate (2026-09-17) · lines 224–235

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Isolation and spectroscopy of a bovine-liver chromium-containing peptide fraction · source_derived_draft · unverified_draft

    ### chromium-chromodulin-isolate The bovine-liver low-molecular-weight isolate contained approximately four Cr(III) ions per peptide, with spectra consistent with carboxylate-supported metal assemblies; one tetranuclear versus two dinuclear assemblies was unresolved. Condition category: normal nutrient_topic: Chromium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Researchers isolated a chromium-binding peptide fraction, but its structure and origin inside living cells were not fully settled. organism: Bovine liver isolate tissue_or_cell_type: Purified fraction outside intact cells experimental_model: Isolation and spectroscopy of a bovine-liver chromium-containing peptide fraction limitations: The paper interpreted the isolate as naturally occurring; later work questioned whether similar low-molecular-weight species arise during extraction. Exact nuclearity was not resolved by this study. exposure: Spectroscopic characterization of an isolate with approximately four Cr(III) ions per peptide evidence_span: {"source_cache": "artifacts/chromium-research/9056266.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "36be61aa6271d3491a4432d31d5ea6524a059fcc1f1ba1e0acac5f175f711a06", "start_char": 0, "end_char": 791, "text_sha256": "36be61aa6271d3491a4432d31d5ea6524a059fcc1f1ba1e0acac5f175f711a06"} [chromium-p9056266] Isolation and characterization of a biologically active chromium oligopeptide from bovine liver. (1997). https://pubmed.ncbi.nlm.nih.gov/9056266/ DOI: 10.1006/abbi.1997.9878
    Complete structured claim and evidence

  3. Added chromium oligopeptide enhanced insulin-stimulated receptor tyrosine-kinase activity by up to eightfold in rat adipocyte membrane fragments; no enhancement occurred without insulin.

    Bovine liver low-molecular-weight chromium-binding isolate / chromodulin candidate → Insulin receptor tyrosine-kinase activity source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/chromium-research/9109644.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "23e955cef071c135f3935f440f4e333d49f494f004ceb22574df717c86bb7283", "start_char": 0, "end_char": 939, "text_sha256": "23e955cef071c135f3935f440f4e333d49f494f004ceb22574df717c86bb7283"}
    experimental_model
    Isolated rat insulin receptor and adipocyte membrane kinase assays
    exposure
    Insulin activation with added low-molecular-weight chromium-binding material
    limitations
    Assay activity is distinct from proof of an endogenous human cofactor. The peptide preparation and its cellular origin remain disputed; chromium is not shown to be an obligatory catalytic metal of INSR.
    nutrient_topic
    Chromium research collection; topical membership is not evidence of a direct dietary effect. · Chromium
    organism
    Rat receptor; isolated chromium oligopeptide preparation
    plain_language
    The preparation amplified an existing insulin signal in this experiment; it did not replace insulin.
    primary_references
    [chromium-p9109644] Chromium oligopeptide activates insulin receptor tyrosine kinase activity. (1997). https://pubmed.ncbi.nlm.nih.gov/9109644/ DOI: 10.1021/bi963154t
    tissue_or_cell_type
    Purified receptor and membrane fragments

    Chromium: transport, insulin signaling, nutrient interactions and essentiality debate (2026-09-17) · lines 263–274

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Isolated rat insulin receptor and adipocyte membrane kinase assays · source_derived_draft · unverified_draft

    ### chromium-chromodulin-kinase-amplification Added chromium oligopeptide enhanced insulin-stimulated receptor tyrosine-kinase activity by up to eightfold in rat adipocyte membrane fragments; no enhancement occurred without insulin. Condition category: normal nutrient_topic: Chromium research collection; topical membership is not evidence of a direct dietary effect. plain_language: The preparation amplified an existing insulin signal in this experiment; it did not replace insulin. organism: Rat receptor; isolated chromium oligopeptide preparation tissue_or_cell_type: Purified receptor and membrane fragments experimental_model: Isolated rat insulin receptor and adipocyte membrane kinase assays limitations: Assay activity is distinct from proof of an endogenous human cofactor. The peptide preparation and its cellular origin remain disputed; chromium is not shown to be an obligatory catalytic metal of INSR. exposure: Insulin activation with added low-molecular-weight chromium-binding material evidence_span: {"source_cache": "artifacts/chromium-research/9109644.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "23e955cef071c135f3935f440f4e333d49f494f004ceb22574df717c86bb7283", "start_char": 0, "end_char": 939, "text_sha256": "23e955cef071c135f3935f440f4e333d49f494f004ceb22574df717c86bb7283"} [chromium-p9109644] Chromium oligopeptide activates insulin receptor tyrosine kinase activity. (1997). https://pubmed.ncbi.nlm.nih.gov/9109644/ DOI: 10.1021/bi963154t
    Complete structured claim and evidence

  4. The isolate increased membrane phosphotyrosine-phosphatase activity in proportion to the amount added, while the isolate itself had no intrinsic phosphatase activity.

    Bovine liver low-molecular-weight chromium-binding isolate / chromodulin candidate → Adipocyte membrane phosphotyrosine phosphatases (identity unresolved) source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/chromium-research/8841143.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "04928cdcbe3e2a282fa43f6a987d1846c6a4e882a6834542b19578b43f8f8322", "start_char": 0, "end_char": 942, "text_sha256": "04928cdcbe3e2a282fa43f6a987d1846c6a4e882a6834542b19578b43f8f8322"}
    experimental_model
    Membrane phosphatase kinetics and inhibitor profiling
    exposure
    Added low-molecular-weight chromium-binding preparation
    limitations
    The phosphatase was not molecularly identified. Inhibitor behavior suggested similarity to PTP1A′ or PTP1B but does not justify assigning this result to a specific gene. Activation here is not proof of universal PTP1B inhibition.
    nutrient_topic
    Chromium research collection; topical membership is not evidence of a direct dietary effect. · Chromium
    organism
    Bovine liver isolate; adipocyte membranes
    plain_language
    This experiment increased a phosphatase activity; the exact enzyme identity remained unresolved.
    primary_references
    [chromium-p8841143] A biologically active form of chromium may activate a membrane phosphotyrosine phosphatase (PTP). (1996). https://pubmed.ncbi.nlm.nih.gov/8841143/ DOI: 10.1021/bi960328y
    tissue_or_cell_type
    Cell-membrane enzyme preparation

    Chromium: transport, insulin signaling, nutrient interactions and essentiality debate (2026-09-17) · lines 289–300

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Membrane phosphatase kinetics and inhibitor profiling · source_derived_draft · unverified_draft

    ### chromium-membrane-phosphatase-activation The isolate increased membrane phosphotyrosine-phosphatase activity in proportion to the amount added, while the isolate itself had no intrinsic phosphatase activity. Condition category: normal nutrient_topic: Chromium research collection; topical membership is not evidence of a direct dietary effect. plain_language: This experiment increased a phosphatase activity; the exact enzyme identity remained unresolved. organism: Bovine liver isolate; adipocyte membranes tissue_or_cell_type: Cell-membrane enzyme preparation experimental_model: Membrane phosphatase kinetics and inhibitor profiling limitations: The phosphatase was not molecularly identified. Inhibitor behavior suggested similarity to PTP1A′ or PTP1B but does not justify assigning this result to a specific gene. Activation here is not proof of universal PTP1B inhibition. exposure: Added low-molecular-weight chromium-binding preparation evidence_span: {"source_cache": "artifacts/chromium-research/8841143.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "04928cdcbe3e2a282fa43f6a987d1846c6a4e882a6834542b19578b43f8f8322", "start_char": 0, "end_char": 942, "text_sha256": "04928cdcbe3e2a282fa43f6a987d1846c6a4e882a6834542b19578b43f8f8322"} [chromium-p8841143] A biologically active form of chromium may activate a membrane phosphotyrosine phosphatase (PTP). (1996). https://pubmed.ncbi.nlm.nih.gov/8841143/ DOI: 10.1021/bi960328y
    Complete structured claim and evidence

What acts on it

  1. The preparation’s ability to enhance insulin-receptor tyrosine-kinase activity depended on its chromium content.

    Trivalent chromium / Cr(III) → Bovine liver low-molecular-weight chromium-binding isolate / chromodulin candidate source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/chromium-research/9109644.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "23e955cef071c135f3935f440f4e333d49f494f004ceb22574df717c86bb7283", "start_char": 0, "end_char": 939, "text_sha256": "23e955cef071c135f3935f440f4e333d49f494f004ceb22574df717c86bb7283"}
    experimental_model
    Isolated rat insulin receptor and adipocyte membrane kinase assays
    exposure
    Insulin activation with added low-molecular-weight chromium-binding material
    limitations
    Assay activity is distinct from proof of an endogenous human cofactor. The peptide preparation and its cellular origin remain disputed; chromium is not shown to be an obligatory catalytic metal of INSR.
    nutrient_topic
    Chromium research collection; topical membership is not evidence of a direct dietary effect. · Chromium
    organism
    Rat receptor; isolated chromium oligopeptide preparation
    plain_language
    Removing the preparation’s metal content reduced its assay effect; that does not establish dietary chromium deficiency in humans.
    primary_references
    [chromium-p9109644] Chromium oligopeptide activates insulin receptor tyrosine kinase activity. (1997). https://pubmed.ncbi.nlm.nih.gov/9109644/ DOI: 10.1021/bi963154t
    tissue_or_cell_type
    Purified receptor and membrane fragments

    Chromium: transport, insulin signaling, nutrient interactions and essentiality debate (2026-09-17) · lines 276–287

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Isolated rat insulin receptor and adipocyte membrane kinase assays · source_derived_draft · unverified_draft

    ### chromium-chromodulin-metal-dependence The preparation’s ability to enhance insulin-receptor tyrosine-kinase activity depended on its chromium content. Condition category: normal nutrient_topic: Chromium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Removing the preparation’s metal content reduced its assay effect; that does not establish dietary chromium deficiency in humans. organism: Rat receptor; isolated chromium oligopeptide preparation tissue_or_cell_type: Purified receptor and membrane fragments experimental_model: Isolated rat insulin receptor and adipocyte membrane kinase assays limitations: Assay activity is distinct from proof of an endogenous human cofactor. The peptide preparation and its cellular origin remain disputed; chromium is not shown to be an obligatory catalytic metal of INSR. exposure: Insulin activation with added low-molecular-weight chromium-binding material evidence_span: {"source_cache": "artifacts/chromium-research/9109644.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "23e955cef071c135f3935f440f4e333d49f494f004ceb22574df717c86bb7283", "start_char": 0, "end_char": 939, "text_sha256": "23e955cef071c135f3935f440f4e333d49f494f004ceb22574df717c86bb7283"} [chromium-p9109644] Chromium oligopeptide activates insulin receptor tyrosine kinase activity. (1997). https://pubmed.ncbi.nlm.nih.gov/9109644/ DOI: 10.1021/bi963154t
    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.

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