Rumigny J F, Maitre M, Cash C, Mandel P
J Neurochem. 1981 Apr;36(4):1433-8. doi: 10.1111/j.1471-4159.1981.tb00583.x.
Rat brain contains two major NADPH-linked aldehyde reductases that can reduce succinate semialdehyde to 4-hydroxybutyrate. One of these enzymes appears to be fairly specific for succinate semialdehyde and is not significantly inhibited by classic aldehyde reductase inhibitors such as barbiturates. The other enzyme can reduce several aromatic aldehydes and is strongly inhibited by barbiturates and branched-chain fatty acids. Using one such inhibitor, it was possible to distinguish between and measure the two enzyme activities separately in various rat brain regions and in subcellular fractions. Both enzymes are mainly cytoplasmic but there is some activity in the synaptosomal fraction. The activity of the specific succinic semialdehyde reductase is highest in the cerebellum, where it represents 21% of the total activity, and lowest in the cortex, where it represents about 11% of the total activity.
大鼠脑内含有两种主要的与NADPH相关的醛还原酶，它们可将琥珀酸半醛还原为4-羟基丁酸。其中一种酶似乎对琥珀酸半醛具有相当的特异性，且不受巴比妥酸盐等经典醛还原酶抑制剂的显著抑制。另一种酶可还原多种芳香醛，并受到巴比妥酸盐和支链脂肪酸的强烈抑制。使用一种这样的抑制剂，能够在大鼠脑的各个区域以及亚细胞组分中分别区分并测量这两种酶的活性。两种酶主要存在于细胞质中，但在突触体组分中也有一些活性。特异性琥珀酸半醛还原酶的活性在小脑最高，占总活性的21%，在皮质最低，约占总活性的11%。
