{"id":"c05589a7-3ee8-51dd-9d02-d9b5a1380f39","stable_key":"c836a883-ac18-5eb2-9971-2f0b542feba8:gsh-reversal-papaya-papain","predicate":"increases_in_recorded_experiment","statement":"Glutathione restored activity of allicin-inhibited papain.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"800d4f8d-00ed-5370-9636-437099b3fc95","mechanism_event_label":"Glutathione restored activity of allicin-inhibited papain.","subject":{"id":"b44c9e27-4bbb-52d3-a022-14cddded5073","slug":"glutathione","display_name":"GSH","entity_type_key":"small_molecule"},"object":{"id":"b0618a7c-edc5-5cc0-8314-d6a77fbece77","slug":"papaya-papain","display_name":"Carica papaya papain","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"800d4f8d-00ed-5370-9636-437099b3fc95","stable_key":"c836a883-ac18-5eb2-9971-2f0b542feba8:gsh-reversal-papaya-papain-event","event_type":"biochemical_relationship","label":"Glutathione restored activity of allicin-inhibited papain.","description":"**Enzyme inhibition and reversal differ by target.** The early purified-enzyme study observed inhibition of papain, bacterial NADP-dependent alcohol dehydrogenase, and horse-liver NAD-dependent alcohol dehydrogenase. Thiols could reactivate the enzymes, but not interchangeably: glutathione restored papain activity, whereas it did not restore the tested bacterial dehydrogenase under those conditions. Dithiothreitol or mercaptoethanol had different reversal profiles. Covalent inhibition is therefore not equivalent to unrecoverable injury, and a general glutathione rescue cannot be assumed for every enzyme. [Rabinkov 1998](https://pubmed.ncbi.nlm.nih.gov/9528659/)","status":"provisional","compartment":null,"participants":[{"entity":{"id":"b44c9e27-4bbb-52d3-a022-14cddded5073","slug":"glutathione","display_name":"GSH","entity_type_key":"small_molecule"},"role":"tested factor","stoichiometry":null,"state_label":"GSH addition after allicin inhibition","sequence_order":0,"notes":""},{"entity":{"id":"b0618a7c-edc5-5cc0-8314-d6a77fbece77","slug":"papaya-papain","display_name":"Carica papaya papain","entity_type_key":"protein"},"role":"measured outcome","stoichiometry":null,"state_label":"increase","sequence_order":1,"notes":""},{"entity":{"id":"85c86fcf-3060-5fae-b567-4f089990ab2d","slug":"allicin","display_name":"Allicin","entity_type_key":"small_molecule"},"role":"prior inhibitor","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary indexed abstract reviewed; full methods, exact concentrations or species-specific attribution remain unextracted unless explicitly stated in the abstract or separately verified publisher text.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_condition","value_text":"prior inhibitory exposure","comparator":"Allicin-inhibited enzyme without effective reductant","unit":null,"notes":"Condition belongs to the full experimental contrast; do not separate a joint intervention.","entity":{"slug":"allicin","display_name":"Allicin","entity_type_key":"small_molecule"}},{"dimension":"experimental_condition","value_text":"added","comparator":"Allicin-inhibited enzyme without effective reductant","unit":null,"notes":"Condition belongs to the full experimental contrast; do not separate a joint intervention.","entity":{"slug":"glutathione","display_name":"GSH","entity_type_key":"small_molecule"}},{"dimension":"experimental_contrast","value_text":"{\"intervention\": \"GSH addition after allicin inhibition\", \"comparator\": \"Allicin-inhibited enzyme without effective reductant\", \"endpoint\": \"Glutathione restored activity of allicin-inhibited papain.\", \"effect_direction\": \"increase\", \"combination\": \"joint\", \"conditions\": [{\"entity_slug\": \"allicin\", \"state\": \"prior inhibitory exposure\"}, {\"entity_slug\": \"glutathione\", \"state\": \"added\"}]}","comparator":null,"unit":null,"notes":"Explicit extracted experimental comparison; source-derived draft.","entity":null},{"dimension":"experimental_model","value_text":"Purified enzyme, prior allicin inhibition, reductant comparison.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"interpretation_status","value_text":"Source-derived extraction of a fact-checked reference; access is explicit, not independent raw-data verification.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Interpret only within the recorded preparation, exposure and comparator. The complete source passage retains qualifications; unspecified doses/timing have not been extracted here. No clinical efficacy, nutrient deficiency or unique molecular mediation is inferred.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Glutathione restored activity of allicin-inhibited papain.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"The mode of action of allicin: trapping of radicals and interaction with thiol containing proteins. | 1998 | DOI 10.1016/s0304-4165(97)00104-9 | PMID 9528659 | https://pubmed.ncbi.nlm.nih.gov/9528659/ | https://doi.org/10.1016/s0304-4165(97)00104-9","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"source_locator","value_text":"Reviewed reference lines 41-41; exact primary location described in quoted passage where extracted.","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"f6d9ac01-3990-57e0-ba55-3042f7dcab15","evidence_kind":"source_excerpt","locator":"Lines 41-41","start_line":41,"end_line":41,"excerpt":"**Enzyme inhibition and reversal differ by target.** The early purified-enzyme study observed inhibition of papain, bacterial NADP-dependent alcohol dehydrogenase, and horse-liver NAD-dependent alcohol dehydrogenase. Thiols could reactivate the enzymes, but not interchangeably: glutathione restored papain activity, whereas it did not restore the tested bacterial dehydrogenase under those conditions. Dithiothreitol or mercaptoethanol had different reversal profiles. Covalent inhibition is therefore not equivalent to unrecoverable injury, and a general glutathione rescue cannot be assumed for every enzyme. [Rabinkov 1998](https://pubmed.ncbi.nlm.nih.gov/9528659/)","model_system":"Purified enzyme, prior allicin inhibition, reductant comparison.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Exact excerpt of the retained AI-assisted reviewed reference; primary sources are cited in primary_references and access scope is retained. Not a verbatim quotation from a primary paper.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"10820a6b-594a-547d-97f9-906ab4cc1d6e","stable_key":"import-c836a883-ac18-5eb2-9971-2f0b542feba8","title":"Allicin: detailed mechanisms of action (reviewed 5 October 2026)","document_type":"imported_text","citation_label":"Original AI-assisted review of primary studies and, where relevant, official regulatory records. Access level is retained per claim. Corrections, null results and unresolved questions remain explicit. Not publisher full text or independent replication.","file_path":"","sha256":"2475d3eb681100a0a34577a47b7cba5b251df866fbd6ce795122ccabee360018","revision_id":"590df96d-2ed1-5763-b04c-bf0e096e603c","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}