大鼠脑中4-氨基丁醛脱氢酶的活性
4-Aminobutyraldehyde dehydrogenase activity in rat brain.
作者信息
Tago K, Kurioka S, Matsuda M
出版信息
J Neurochem. 1982 Sep;39(3):803-9. doi: 10.1111/j.1471-4159.1982.tb07963.x.
An enzyme with NAD+-dependent 4-aminobutyraldehyde dehydrogenase activity was purified about 360-fold from rat brain extract. AMP-Sepharose chromatography was effective in separating the enzyme from other NAD+-dependent aldehyde dehydrogenases included in the extract. The KmS for the substrates NAD+ and 4-aminobutyraldehyde were 4.8 x 10(-4) and 8.3 x 10(-5) M, respectively. The pH optimum for the enzyme was about 8.0. The ratio of activities toward 4-aminobutyraldehyde, propionaldehyde, succinate semialdehyde, and benzaldehyde was 1.00:0.17:0.24:0.09:0.03 when the activity toward 4-aminobutyraldehyde was set equal to 1.00. The enzyme activity in subcellular fractions of rat brain was localized in cytosol.
从大鼠脑提取物中纯化出一种具有NAD⁺依赖性4-氨基丁醛脱氢酶活性的酶，纯化倍数约为360倍。AMP-琼脂糖层析能有效地将该酶与提取物中其他NAD⁺依赖性醛脱氢酶分离。该酶对底物NAD⁺和4-氨基丁醛的Km值分别为4.8×10⁻⁴和8.3×10⁻⁵M。该酶的最适pH约为8.0。当以对4-氨基丁醛的活性为1.00时，该酶对4-氨基丁醛、丙醛、琥珀酸半醛和苯甲醛的活性比为1.00:0.17:0.24:0.09:0.03。大鼠脑亚细胞组分中的酶活性定位于胞质溶胶中。
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