Kaufman E E, Nelson T, Miller D, Stadlan N
Laboratory of Cerebral Metabolism, National Institute of Mental Health, Bethesda, Maryland 20892.
J Neurochem. 1988 Oct;51(4):1079-84. doi: 10.1111/j.1471-4159.1988.tb03071.x.
An antibody that inhibits over 95% of the cytosolic NADP+-dependent gamma-hydroxybutyrate (GHB) dehydrogenase activity of either rat brain or kidney was found to inhibit only approximately 50% of the conversion of [1-14C]GHB to 14CO2 by rat kidney homogenate. A similar result was obtained with sodium valproate, a potent inhibitor of GHB dehydrogenase. The mitochondrial fraction from rat brain and kidney was found to catalyze the conversion of [1-14C]GHB to 14CO2. The dialyzed mitochondrial fraction also catalyzed the oxidation of GHB to succinic semialdehyde (SSA) in a reaction that did not require added NAD+ or NADP+ and which was not inhibited by sodium valproate. The enzyme from the mitochondrial fraction which converts GHB to SSA appears to be distinct from the NADP+-dependent cytosolic oxidoreductase which catalyzes this reaction.
一种能抑制大鼠脑或肾胞质中超过95%的NADP⁺依赖性γ-羟基丁酸（GHB）脱氢酶活性的抗体，被发现只能抑制大鼠肾匀浆将[1-¹⁴C]GHB转化为¹⁴CO₂的过程的约50%。用丙戊酸钠（一种强效的GHB脱氢酶抑制剂）也得到了类似的结果。发现大鼠脑和肾的线粒体部分能催化[1-¹⁴C]GHB转化为¹⁴CO₂。透析后的线粒体部分也能在一个不需要添加NAD⁺或NADP⁺且不受丙戊酸钠抑制的反应中催化GHB氧化为琥珀酸半醛（SSA）。线粒体部分中能将GHB转化为SSA的酶似乎与催化该反应的NADP⁺依赖性胞质氧化还原酶不同。
