Selectivity in the binding of psychotropic drugs to the variants of alpha-1 acid glycoprotein.
Details
Serval ID
serval:BIB_B6ED57D9EAD8
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Selectivity in the binding of psychotropic drugs to the variants of alpha-1 acid glycoprotein.
Journal
Naunyn-schmiedeberg's Archives of Pharmacology
ISSN
0028-1298 (Print)
ISSN-L
0028-1298
Publication state
Published
Issued date
1988
Peer-reviewed
Oui
Volume
337
Number
2
Pages
220-224
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov'tPublication Status: ppublish
Abstract
The S- and F-forms of alpha-1 acid glycoprotein (AAG) variants have been isolated by isoelectric focusing with immobilines from commercially available AAG. In equilibrium dialysis experiments using a multicompartmental system, a higher affinity for various basic drugs has been found with S- in comparison with F-AAG: Amitriptyline, nortriptyline, imipramine, desipramine, trimipramine, methadone, thioridazine, clomipramine, desmethylclomipramine, and maprotiline. The selectivity (binding to S- vs. F-AAG) is the most pronounced for methadone and the lowest for thioridazine, while it is absent for the acidic drug mephenytoin.
Keywords
Amitriptyline/metabolism, Clomipramine/metabolism, Desipramine/metabolism, Hydrogen-Ion Concentration, Imipramine/metabolism, Maprotiline/metabolism, Methadone/metabolism, Orosomucoid/analogs & derivatives, Orosomucoid/metabolism, Psychotropic Drugs/metabolism, Thioridazine/metabolism, Trimipramine/metabolism
Pubmed
Web of science
Create date
01/03/2013 10:41
Last modification date
20/08/2019 16:25
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