Hopkinson D A, Santisteban I, Povey S, Smith M
Alcohol. 1985 Jan-Feb;2(1):73-8. doi: 10.1016/0741-8329(85)90019-9.
ALDH isozymes have been characterized in terms of substrate and coenzyme specificity, heat stability, tissue distribution and electrophoretic properties. The activity of the isozymes has also been examined in rodent-human somatic cell hybrids in order to map the structural genes to specific chromosomes and to study the control of gene expression. One isozyme, designated ALDH3, which is very active against benzaldehyde, was found to show variable expression in hybrids made between rat hepatoma cells and human fibroblasts or fetal liver. Segregation analysis of these hybrids indicates that the structural locus for human ALDH3 may be on chromosome 17. The expression of rodent ALDH3 in these hybrids was extremely variable and not correlated with the appearance of the human enzyme. In hybrids expressing human and rodent ALDH3 no heteromeric isozymes were observed. The human "cytosolic" ALDH1 and "mitochondrial" ALDH2 isozymes did not appear to be expressed in any of the somatic cell hybrids examined.
已根据底物和辅酶特异性、热稳定性、组织分布及电泳特性对醛脱氢酶同工酶进行了表征。还在啮齿动物 - 人类体细胞杂种中检测了同工酶的活性，以便将结构基因定位到特定染色体并研究基因表达的调控。发现一种对苯甲醛具有高活性的同工酶，命名为ALDH3，在大鼠肝癌细胞与人成纤维细胞或胎儿肝脏之间形成的杂种中表现出可变表达。对这些杂种的分离分析表明，人类ALDH3的结构基因座可能位于17号染色体上。这些杂种中啮齿动物ALDH3的表达极其可变，且与人类酶的出现无关。在表达人类和啮齿动物ALDH3的杂种中未观察到异源同工酶。在所检测的任何体细胞杂种中，人类“胞质”ALDH1和“线粒体”ALDH2同工酶似乎均未表达。
