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(2013). https://pubmed.ncbi.nlm.nih.gov/23650179/ DOI: 10.1002/mnfr.201200797","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Microsomal enzyme preparation","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"766ac3d8-76e9-507a-ae9d-bf390305d711","evidence_kind":"source_excerpt","locator":"Lines 467-478","start_line":467,"end_line":478,"excerpt":"### ve-transport-alpha-does-not-activate-k1-catabolism\nAlpha-tocopherol did not increase phylloquinone omega-hydroxylation in CYP4F2 microsomes; the study reported a slight decrease in apparent phylloquinone Vmax.\nCondition category: normal\nnutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: This assay did not support faster vitamin K1 breakdown caused by alpha-tocopherol.\norganism: Human protein in insect microsomes\ntissue_or_cell_type: Microsomal enzyme preparation\nexperimental_model: Recombinant human CYP4F2 co-substrate kinetics\nlimitations: Does not exclude other mechanisms of vitamin E–K interaction in animals or humans.\nexposure: Labeled phylloquinone 0–50 µM with RRR-alpha-tocopherol 0–50 µM or SRR-alpha-tocopherol 0–100 µM; 30 min, 37 °C, 1 mM NADPH.\ncross_nutrient: true\n[farley2013] ω-Hydroxylation of phylloquinone by CYP4F2 is not increased by α-tocopherol. 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