Titre
Binding of amitriptyline to alpha 1-acid glycoprotein and its variants.
Type
article
Institution
UNIL/CHUV/Unisanté + institutions partenaires
Périodique
Auteur(s)
Eap, C.B.
Auteure/Auteur
Cuendet, C.
Auteure/Auteur
Baumann, P.
Auteure/Auteur
Liens vers les personnes
Liens vers les unités
ISSN
0022-3573
Statut éditorial
Publié
Date de publication
1988
Volume
40
Numéro
11
Première page
767
Dernière page/numéro d’article
770
Peer-reviewed
Oui
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov'tPublication Status: ppublish
Résumé
Binding studies have been performed between amitriptyline and i) native alpha 1-acid glycoprotein (AAG); ii) its desialylated form; iii) its two variants, S-AAG and F-AAG; and iv) a mixture of S-AAG and F-AAG. Scatchard analysis revealed the presence of two classes of binding sites on AAG. For native AAG, the first class (of high affinity) has an association constant (Ka1) of 1.5 x 10(6) L mol-1 and a number of binding sites per mole of protein (n1) of 0.25, while the second class (of low affinity) has a Ka2 of 3.2 x 10(4) L mol-1 and a n2 of 0.94. Similar data were found for desialylated AAG. S-AAG and F-AAG do not differ in their association constants measured with amitriptyline, but in their number of binding sites per mole of protein (n): S-AAG: n1 = 0.56, n2 = 0.52; F-AAG: n1 = 0.17, n2 = 0.71. These results confirm those of a previous study, in which a higher affinity of S-AAG towards various basic drugs in comparison with F-AAG has been found.
PID Serval
serval:BIB_61F900250115
PMID
Date de création
2013-03-01T09:02:44.485Z
Date de création dans IRIS
2025-05-21T00:19:46Z