Suppr超能文献

精神药物与α-1酸性糖蛋白变体结合的选择性。

Selectivity in the binding of psychotropic drugs to the variants of alpha-1 acid glycoprotein.

作者信息

Eap C B, Cuendet C, Baumann P

机构信息

Clinique Psychiatrique Universitaire de Lausanne, Hôpital de Cery, Prilly, Switzerland.

出版信息

Naunyn Schmiedebergs Arch Pharmacol. 1988 Feb;337(2):220-4. doi: 10.1007/BF00169251.

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.

摘要

已通过使用固定化电解质的等电聚焦从市售α-1酸性糖蛋白(AAG)中分离出其S型和F型变体。在使用多隔室系统的平衡透析实验中,与F-AAG相比,发现S-AAG对各种碱性药物具有更高的亲和力:阿米替林、去甲替林、丙咪嗪、地昔帕明、曲米帕明、美沙酮、硫利达嗪、氯米帕明、去甲氯米帕明和马普替林。美沙酮的选择性(与S-AAG和F-AAG的结合)最为明显,硫利达嗪的选择性最低,而酸性药物美芬妥英则不存在这种选择性。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验