Selectivity in the binding of psychotropic drugs to the variants of alpha-1 acid glycoprotein.
| Data(s) |
1988
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|---|---|
| Resumo |
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. |
| Identificador |
https://serval.unil.ch/?id=serval:BIB_B6ED57D9EAD8 isbn:0028-1298 (Print) pmid:3368020 isiid:A1988M549600014 doi: |
| Idioma(s) |
en |
| Fonte |
Naunyn-schmiedeberg's Archives of Pharmacology, vol. 337, no. 2, pp. 220-224 |
| Palavras-Chave | #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 |
| Tipo |
info:eu-repo/semantics/article article |
