Meier-Tackmann D, Agarwal D P, Saha N, Goedde H W
Enzyme. 1984;32(3):170-7. doi: 10.1159/000469471.
Human stomach aldehyde dehydrogenase (ALDH) isozymes were screened in random autopsy specimens from 66 North German and 33 Chinese individuals. Three ALDH isozymes were identified, which differed in their electrophoretic mobility, affinity to acetaldehyde, propionaldehyde, furfural, and to NAD+ as coenzyme as well as in inhibition by disulfiram, pH optimum and heat stability. While all the German stomach specimens showed ALDH I, ALDH II, and ALDH III isozymes, these isozymes were found in 68, 88, and 99% of the Chinese samples, respectively. The electrophoretic resolution of ALDH III into different activity bands is apparently due to the artefactual formation of secondary isozymes rather than to the existence of genetic variants.
在66名德国北部人和33名中国人的随机尸检标本中筛选了人类胃醛脱氢酶（ALDH）同工酶。鉴定出三种ALDH同工酶，它们在电泳迁移率、对乙醛、丙醛、糠醛的亲和力以及对作为辅酶的NAD+的亲和力方面存在差异，同时在双硫仑抑制作用、最适pH值和热稳定性方面也有所不同。虽然所有德国胃标本都显示有ALDH I、ALDH II和ALDH III同工酶，但这些同工酶分别在68%、88%和99%的中国样本中被发现。ALDH III电泳分离成不同活性带显然是由于二级同工酶的人为形成，而非遗传变异的存在。
