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(1996). https://pubmed.ncbi.nlm.nih.gov/8769129/ DOI: 10.1006/bbrc.1996.1165","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified thioredoxin reductases","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"731ba9be-fd64-5b2f-8eed-e25040443d73","evidence_kind":"source_excerpt","locator":"Lines 754-765","start_line":754,"end_line":765,"excerpt":"### ala-thioredoxin-reductase-dhla\nPurified mammalian thioredoxin reductases, including enzyme from human placenta, catalyzed NADPH-dependent lipoic-acid reduction.\nCondition category: normal\nnutrient_topic: Alpha-lipoic acid research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The thioredoxin system provides another route to DHLA.\norganism: Human placenta, calf tissues and rat liver\ntissue_or_cell_type: Purified thioredoxin reductases\nexperimental_model: Purified mammalian thioredoxin reductase assays\nlimitations: Isoform identity was not resolved as a specific human TXNRD gene in the indexed abstract; assay rate comparisons are not tissue-wide flux rankings.\nexposure: NADPH-dependent lipoate/lipoamide reduction\nevidence_span: {\"source_cache\": \"artifacts/ala-research/8769129.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"9ba6524ef04fdc03c0a6d108325b8a96fe7ad0748be4d7056e694b5afa2a8499\", \"start_char\": 0, \"end_char\": 1307, \"text_sha256\": \"9ba6524ef04fdc03c0a6d108325b8a96fe7ad0748be4d7056e694b5afa2a8499\"}\n[ala-p8769129] Efficient reduction of lipoamide and lipoic acid by mammalian thioredoxin reductase. 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