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(1999). https://pubmed.ncbi.nlm.nih.gov/10608822/ DOI: 10.1074/jbc.274.53.37658","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Endothelial NOS enzyme preparation","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"552ce326-c5d4-553d-a4e8-d6a8c7c62c12","evidence_kind":"source_excerpt","locator":"Lines 580-591","start_line":580,"end_line":591,"excerpt":"### citrulline-nos-dimer\nBH4 plus arginine shifted human eNOS toward dimers during low-temperature electrophoresis.\nCondition category: normal\nnutrient_topic: Citrulline research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Cofactor and substrate helped stabilize the paired enzyme structure.\norganism: Human NOS3 expressed in yeast\ntissue_or_cell_type: Endothelial NOS enzyme preparation\nexperimental_model: Purified recombinant enzyme activity and cofactor analysis\nlimitations: Biochemical cofactor findings do not show that extra dietary cofactors increase NO in healthy people.\nexposure: Arginine substrate; BH4, FAD, FMN, heme, iron and zinc measurements\nevidence_span: {\"source_cache\": \"artifacts/citrulline-research/10608822.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"1600b193cc63f30b204285729710bb81f34bc2918a8ca7f97aa97bc4acd998fd\", \"start_char\": 0, \"end_char\": 2100, \"text_sha256\": \"1600b193cc63f30b204285729710bb81f34bc2918a8ca7f97aa97bc4acd998fd\"}\n[citrulline-p10608822] Characterization of recombinant human endothelial nitric-oxide synthase purified from the yeast Pichia pastoris. 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