喹啉和喹哪啶作为天然存在的对A型单胺氧化酶具有特异性的抑制剂。

Quinoline and quninaldine as naturally occurring inhibitors specific for type A monoamine oxidase.

作者信息

Naoi M, Nagatsu T

出版信息

Life Sci. 1987 Mar 16;40(11):1075-82. doi: 10.1016/0024-3205(87)90570-4.

Abstract

Type A monoamine oxidase (MAO-A) in human placental mitochondria was competitively inhibited by naturally occurring substances, quinoline and quinaldine, using kynuramine as substrate. Quinoline had a higher affinity for MAO than kynuramine. MAO-A in human brain synaptosomal mitochondria was also competitively inhibited by quinoline, while type B MAO (MAO-B) was reversibly and non-competitively inhibited by quinoline. Quinoline inhibited MAO-A much more potently than MAO-B. Of several compounds structurally similar to quinoline, isoquinoline noncompetitively inhibited MAO-A and -B activity.

摘要

以犬尿胺为底物时，人胎盘线粒体中的A型单胺氧化酶（MAO-A）受到天然存在的物质喹啉和喹哪啶的竞争性抑制。喹啉对MAO的亲和力高于犬尿胺。人脑海突触体线粒体中的MAO-A也受到喹啉的竞争性抑制，而B型单胺氧化酶（MAO-B）则受到喹啉的可逆性非竞争性抑制。喹啉对MAO-A的抑制作用比对MAO-B强得多。在几种与喹啉结构相似的化合物中，异喹啉非竞争性抑制MAO-A和MAO-B的活性。