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(1983). https://pubmed.ncbi.nlm.nih.gov/6883721/ DOI: 10.1016/0009-8981(83)90096-7","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Serum and biochemical disease phenotype","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"8b39e9cd-eb8c-5338-b90a-532fa79aa5a5","evidence_kind":"source_excerpt","locator":"Lines 455-466","start_line":455,"end_line":466,"excerpt":"### b7-btd-recycling\nBiotinidase releases biotin from its linkage to the epsilon-amino group of lysine, allowing the cofactor to be reused.\nCondition category: normal\nnutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Biotinidase recovers biotin after biotin-containing material is broken down.\norganism: Homo sapiens\ntissue_or_cell_type: Serum and biochemical disease phenotype\nexperimental_model: Serum enzyme assays in 5 children with late-onset multiple carboxylase deficiency and family members\nlimitations: Early small case series; the serum enzyme phenotype is genetic machinery impairment, not proof of low dietary intake.\nexposure: Inherited deficiency; patient/control comparison\nevidence_span: {\"source_cache\": \"artifacts/biotin-research/6883721.abstract.txt\", \"locator\": \"Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"0f881dd651d45537377661fc515239c3babb7160c3dbd53b8b0611ba33625aaa\", \"start_char\": 0, \"end_char\": 1500, \"text_sha256\": \"0f881dd651d45537377661fc515239c3babb7160c3dbd53b8b0611ba33625aaa\"}\n[b7-p6883721] Biotinidase deficiency: the enzymatic defect in late-onset multiple carboxylase deficiency. 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