Tenne M, Finberg J P, Youdim M B, Ulitzur S
J Neurochem. 1985 May;44(5):1378-84. doi: 10.1111/j.1471-4159.1985.tb08773.x.
The in vivo luminescence of an aldehyde-requiring mutant of the luminous bacteria Vibrio harveyi (M42) increases dramatically upon the addition of long-chain aliphatic aldehydes (C8-C16). The intensity of this luminescence is linearly related to aldehyde concentration. This property was utilized for the determination of monoamine oxidase activity using n-octylamine and n-decylamine as substrates, which are converted by monoamine oxidase to n-octylaldehyde and n-decylaldehyde, respectively. The addition of the amine to a suspension containing rat liver mitochondria and M42 cells initiated a luminescence that was directly proportional to monoamine oxidase activity according to two parameters: (1) the rate of the initial increase in luminescence and (2) the final "steady-state" level of luminescence. The new assay has advantages of high sensitivity, rapidity, the possibility to perform discontinuous as well as continuous monitoring of monoamine oxidase activity, and applicability to turbid preparations.
哈维氏弧菌（M42）的一种需醛突变体在添加长链脂肪醛（C8 - C16）后，其体内发光显著增强。这种发光强度与醛浓度呈线性关系。利用这一特性，以正辛胺和正癸胺为底物测定单胺氧化酶活性，单胺氧化酶分别将它们转化为正辛醛和正癸醛。将胺添加到含有大鼠肝线粒体和M42细胞的悬浮液中会引发发光，根据两个参数，该发光与单胺氧化酶活性成正比：（1）发光初始增加速率；（2）最终的“稳态”发光水平。这种新的测定方法具有灵敏度高、速度快、能够对单胺氧化酶活性进行间断和连续监测以及适用于浑浊制剂等优点。
