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บรรทัด 21:
| melting_high = 281
| protein_bound = 15–40%
| metabolism = [[CYP2D6]],<ref name="FDA Pharmacokinetics" /> [[Dopamine β-hydroxylase|DBH]],<ref name="Substituted amphetamines, FMO, and DBH" /><ref name="DBH amph primary" /> [[Flavin-containing monooxygenase 3|FMO3]]<ref name="Substituted amphetamines, FMO, and DBH" /><ref name="FMO" /><ref name="FMO3-Primary" />
| elimination_half-life = 12h average for d-isomer, 13h for l-isomer
| excretion = [[Renal]]; significant portion unaltered
บรรทัด 47:
== อ้างอิง ==
{{รายการอ้างอิง
<ref name="FDA Pharmacokinetics">{{cite web | title = Adderall XR Prescribing Information | url = http://www.accessdata.fda.gov/drugsatfda_docs/label/2013/021303s026lbl.pdf | pages = 12–13 | publisher = Shire US Inc | work = United States Food and Drug Administration |date=December 2013 | access-date = 30 December 2013 }}</ref>
<ref name="Substituted amphetamines, FMO, and DBH">{{cite book | author = Glennon RA |veditors=Lemke TL, Williams DA, Roche VF, Zito W | title=Foye's principles of medicinal chemistry | date=2013 | publisher=Wolters Kluwer Health/Lippincott Williams & Wilkins | location=Philadelphia, USA | isbn=9781609133450 | pages=646–648 | edition=7th | section-url=https://books.google.com/books?id=Sd6ot9ul-bUC&pg=PA646 | section=Phenylisopropylamine stimulants: amphetamine-related agents | quote=The simplest unsubstituted phenylisopropylamine, 1-phenyl-2-aminopropane, or amphetamine, serves as a common structural template for hallucinogens and psychostimulants. Amphetamine produces central stimulant, anorectic, and sympathomimetic actions, and it is the prototype member of this class (39). ... The phase 1 metabolism of amphetamine analogs is catalyzed by two systems: cytochrome P450 and flavin monooxygenase. ... Amphetamine can also undergo aromatic hydroxylation to ''p''-hydroxyamphetamine. ... Subsequent oxidation at the benzylic position by DA β-hydroxylase affords ''p''-hydroxynorephedrine. Alternatively, direct oxidation of amphetamine by DA β-hydroxylase can afford norephedrine.}}</ref>
<ref name="DBH amph primary">{{cite journal | author = Taylor KB | title = Dopamine-beta-hydroxylase. Stereochemical course of the reaction | journal = Journal of Biological Chemistry | volume = 249 | issue = 2 | pages = 454–458 | date = January 1974 | pmid = 4809526 | access-date = 6 November 2014 | url = http://www.jbc.org/content/249/2/454.full.pdf | quote = Dopamine-β-hydroxylase catalyzed the removal of the pro-R hydrogen atom and the production of 1-norephedrine, (2''S'',1''R'')-2-amino-1-hydroxyl-1-phenylpropane, from d-amphetamine. }}</ref>
<ref name="FMO">{{cite journal |vauthors=Krueger SK, Williams DE | title = Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism | journal = Pharmacology & Therapeutics | volume = 106 | issue = 3 | pages = 357–387 |date=June 2005 | pmid = 15922018 | pmc = 1828602 | doi = 10.1016/j.pharmthera.2005.01.001}}<br />[https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1828602/table/T5/ Table 5: N-containing drugs and xenobiotics oxygenated by FMO]</ref>
<ref name="FMO3-Primary">{{cite journal |vauthors=Cashman JR, Xiong YN, Xu L, Janowsky A | title = N-oxygenation of amphetamine and methamphetamine by the human flavin-containing monooxygenase (form 3): role in bioactivation and detoxication | journal = Journal of Pharmacology and Experimental Therapeutics | volume = 288 | issue = 3 | pages = 1251–1260 | date = March 1999 |pmid = 10027866 }}</ref>
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