Jones K H, Lindahl R, Baker D C, Timkovich R
J Biol Chem. 1987 Aug 15;262(23):10911-3.
The stereospecificity of hydride transfer to NAD+ by several forms of rat liver aldehyde dehydrogenase was determined by a nuclear magnetic resonance method. The forms included several mitochondrial and microsomal isozymes from normal liver, as well as isozymes from xenobiotic-treated and tumor cells. The proton added to NAD+ comes exclusively from the aldehyde substrate and in all cases was A (pro-R)-stereospecific.
采用核磁共振法测定了几种大鼠肝脏醛脱氢酶将氢负离子转移至NAD⁺的立体专一性。这些酶形式包括正常肝脏的几种线粒体和微粒体同工酶，以及经外源化合物处理的细胞和肿瘤细胞中的同工酶。添加到NAD⁺上的质子仅来自醛底物，且在所有情况下都是A（前-R）立体专一性的。
