Zhu H, Piletz J E
University of Mississippi Medical Center, Jackson, Mississippi 39216, USA.
Ann N Y Acad Sci. 2003 Dec;1009:347-52. doi: 10.1196/annals.1304.044.
An I(2) imidazoline binding site on monoamine oxidase-B (MAO-B) is known to be encoded by a noncatalytic part of the enzyme, different from that which recognizes mechanism-based inhibitors. Herein, the relationship between I(2)-imidazoline binding sites and MAO-B activity has been assessed using a semi-purified source of MAO-B: platelet mitochondrial membranes. A positive correlation between I(2) sites and MAO-B activity was observed (r = 0.61, P = 0.0016) among 24 human subjects. Nevertheless, the variance in MAO-B activity cannot be completely accounted for in relation to I(2) sites. Therefore, I(2) density and MAO-B activity are only weakly correlated in platelets.
已知单胺氧化酶-B（MAO-B）上的I(2)咪唑啉结合位点由该酶的非催化部分编码，这与识别基于机制的抑制剂的部分不同。在此，使用MAO-B的半纯化来源：血小板线粒体膜，评估了I(2) - 咪唑啉结合位点与MAO-B活性之间的关系。在24名人类受试者中观察到I(2)位点与MAO-B活性之间存在正相关（r = 0.61，P = 0.0016）。然而，MAO-B活性的差异不能完全用I(2)位点来解释。因此，I(2)密度与血小板中的MAO-B活性仅呈弱相关。
