Shekhar C, Mayanil K, Baquer N Z
Biochem Pharmacol. 1982 Dec 1;31(23):3925-7. doi: 10.1016/0006-2952(82)90311-2.
A substantial percentage of monoamine oxidase activity was found in the soluble fraction of rat brain homogenates. The enzyme was not inhibited in vivo by high doses of clorgyline and deprenyl (12 mg/kg for 2 hr). Monoamine oxidase activity associated with the soluble fraction did not show the usual biphasic dose-response kinetics with clorgyline when kynuramine was used as the substrate. The present data show that there may be a new form of monoamine oxidase associated with the soluble fraction of the cell which has properties different from the two well-known monoamine oxidases A and B.
在大鼠脑匀浆的可溶部分发现了相当大比例的单胺氧化酶活性。该酶在体内不受高剂量氯吉兰和司来吉兰（12毫克/千克，持续2小时）的抑制。当以犬尿胺为底物时，与可溶部分相关的单胺氧化酶活性未显示出氯吉兰常见的双相剂量反应动力学。目前的数据表明，可能存在一种与细胞可溶部分相关的新型单胺氧化酶，其性质不同于两种知名的单胺氧化酶A和B。
