Paterson L M, Tyacke R J, Nutt D J, Hudson A L
Psychopharmacology Unit, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, UK.
Ann N Y Acad Sci. 2003 Dec;1009:353-6. doi: 10.1196/annals.1304.045.
I(2) site-selective compounds are known to interact with and inhibit monoamine oxidase (MAO), but it remains unclear as to whether this interaction occurs through an allosteric or competitive interaction. This study used the new selective, irreversible I(2) ligand BU99006, to clarify the relationship between MAO and the I(2) binding sites (I(2)-BS). Results demonstrate that irreversible binding of BU99006 to rat brain membranes does not inhibit the enzyme or interfere with its interaction with other imidazoline enzyme inhibitors. This finding suggests that the I(2) sites that react with BU99006 are not those implicated in MAO inhibition and points to the existence of at least two distinct I(2) binding proteins.
已知I(2)位点选择性化合物可与单胺氧化酶（MAO）相互作用并抑制该酶，但这种相互作用是通过变构还是竞争性相互作用发生仍不清楚。本研究使用新型选择性、不可逆的I(2)配体BU99006，以阐明MAO与I(2)结合位点（I(2)-BS）之间的关系。结果表明，BU99006与大鼠脑膜的不可逆结合不会抑制该酶，也不会干扰其与其他咪唑啉酶抑制剂的相互作用。这一发现表明，与BU99006反应的I(2)位点并非参与MAO抑制作用的位点，这表明至少存在两种不同的I(2)结合蛋白。
