Spironolakton: Perbedaan antara revisi

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| bioavailability = 60–90%<ref name="Sica2005" >{{cite journal|last1=Sica|first1=Domenic A.|title=Pharmacokinetics and Pharmacodynamics of Mineralocorticoid Blocking Agents and their Effects on Potassium Homeostasis|journal=Heart Failure Reviews|volume=10|issue=1|year=2005|pages=23–29|issn=1382-4147|doi=10.1007/s10741-005-2345-1|pmid=15947888}}</ref><ref name="pmid18729003">{{cite journal | vauthors = Maron BA, Leopold JA | title = Mineralocorticoid receptor antagonists and endothelial function | journal = Curr Opin Investig Drugs | volume = 9 | issue = 9 | pages = 963–9 | year = 2008 | pmid = 18729003 | pmc = 2967484 | doi = | url = }}</ref><ref name="CaroneOxberry2017">{{cite journal|last1=Carone|first1=Laura|last2=Oxberry|first2=Stephen G.|last3=Twycross|first3=Robert|last4=Charlesworth|first4=Sarah|last5=Mihalyo|first5=Mary|last6=Wilcock|first6=Andrew|title=Spironolactone|journal=Journal of Pain and Symptom Management|volume=53|issue=2|year=2017|pages=288–292|issn=0885-3924|doi=10.1016/j.jpainsymman.2016.12.320|pmid=28024992}}</ref>
| protein_bound = Spironolactone: 88% (pada [[human serum albumin|albumin]] dan {{abbrlink|AGP|alpha-1-acid glycoprotein}})<ref name="TakamuraMaruyama1997" >{{cite journal|last1=Takamura|first1=Norito|last2=Maruyama|first2=Toru|last3=Ahmed|first3=Shamim|last4=Suenaga|first4=Ayaka|last5=Otagiri|first5=Masaki |title=Interactions of Aldosterone Antagonist Diuretics with Human Serum Proteins |journal=Pharmaceutical Research|volume=14|issue=4|year=1997|pages=522–526|issn=0724-8741 |doi=10.1023/A:1012168020545|pmid=9144743}}</ref><br />Canrenone: 99.2% (pada albumin)<ref name="TakamuraMaruyama1997" />
| metabolism = [[Liver]], lainnya:<br />• [[Deacetylation]] via {{abbrlink|CES|carboxylesterase}}<br />• ''S''-[[Oxidation|Oxygenation]] via {{abbrlink|FOM|flavin-containing monooxygenase}}<br />• ''S''-[[Methylation]] via {{abbrlink|TMT|thiol S-methyltransferase}}<br />• [[Dethioacetylation]]<br />• [[Hydroxylation]] via [[CYP3A4]]<br />• [[Lactone]] [[hydrolysis]] via [[PON3]])<ref name="Sica2005" /><ref name="pmid18729003" /><ref name="Parkinson2001">{{cite book|author=Andrew Parkinson|title=Biotransformation of Xenobiotics|url=https://books.google.com/books?id=pAovcgAACAAJ|year=2001|publisher=McGraw-Hill|pages=137–138, 169, 171, 180, 195, 208}}</ref><ref name="Klaassen2007">{{cite book|author=Curtis D. Klaassen|title=Casarett & Doull's Toxicology: The Basic Science of Poisons, Seventh Edition|url=https://books.google.com/books?id=4yi7-j48uhIC|date=11 December 2007|publisher=McGraw Hill Professional|isbn=978-0-07-159351-9|page=173|quote=Some P450 enzymes (such as the rate enzyme CYP2A1) preferentially catalyze the 6α-hydroxylation reaction, whereas other P450 enzymes (such as the CYP3A enzymes in all mammalian species) preferentially catalyze the 6β-hydroxylation reaction (which is a major route of hepatic steroid biotransformation).}}</ref><ref name="pmid7895608">{{cite journal | vauthors = Los LE, Pitzenberger SM, Ramjit HG, Coddington AB, Colby HD | title = Hepatic metabolism of spironolactone. Production of 3-hydroxy-thiomethyl metabolites | journal = Drug Metab. Dispos. | volume = 22 | issue = 6 | pages = 903–8 | date = 1994 | pmid = 7895608 | doi = | url = http://dmd.aspetjournals.org/content/22/6/903}}</ref><ref name="BlackElliott2006">{{cite book|author1=Henry R. Black|author2=William Elliott|title=Hypertension: A Companion to Braunwald's Heart Disease|url=https://books.google.com/books?id=42Fcmne6_w8C&pg=PA295|date=28 December 2006|publisher=Elsevier Health Sciences|isbn=978-1-4377-1078-6|pages=295–}}</ref> <ref name="pmid14579013">{{cite journal | vauthors = Draganov DI, La Du BN | title = Pharmacogenetics of paraoxonases: a brief review | journal = Naunyn Schmiedebergs Arch. Pharmacol. | volume = 369 | issue = 1 | pages = 78–88 | date = January 2004 | pmid = 14579013 | doi = 10.1007/s00210-003-0833-1 | url = | hdl = 2027.42/46312 }}</ref>
| metabolites = {{abbrlink|7α-TS|7α-Thiospironolactone}}, {{abbrlink|7α-TMS|7α-thiomethylspironolactone}}, {{abbrlink|6β-OH-7α-TMS|6β-hydroxy-7α-thiomethylspironolactone}}, [[canrenone]], lainnya<ref name="Sica2005" /><ref name="pmid18729003" /><ref name="SzaszBudvari-Barany1990" /><br />(All three active)<ref name="McDonaghGardner2011">{{cite book|author1=Theresa A. McDonagh|author2=Roy S. Gardner|author3=Andrew L. Clark|author4=Henry Dargie|title=Oxford Textbook of Heart Failure|url=https://books.google.com/books?id=KDDCiTQyGLsC&pg=PA403|date=14 July 2011|publisher=OUP Oxford|isbn=978-0-19-957772-9|pages=403–|url-status=live|archiveurl=https://web.archive.org/web/20170327090209/https://books.google.com/books?id=KDDCiTQyGLsC&pg=PA403|archivedate=27 March 2017}}</ref>
| elimination_half-life = Spironolactone: 1.4 jam<ref name="Sica2005" /><br />{{abbrlink|7α-TMS|7α-thiomethylspironolactone}}: 13.8 jam<ref name="Sica2005" /><br />{{abbrlink|6β-OH-7α-TMS|6β-hydroxy-7α-thiomethylspironolactone}}: 15.0 jam<ref name="Sica2005" /><br />[[Canrenone]]: 16.5 jam<ref name="Sica2005" />