Evces S, Lindahl R
Department of Biology, University of Alabama, Tuscaloosa.
Arch Biochem Biophys. 1989 Nov 1;274(2):518-24. doi: 10.1016/0003-9861(89)90465-7.
Aldehyde dehydrogenase has been purified from rat cornea in a single step. The enzyme is a class 3 aldehyde dehydrogenase. Cornea aldehyde dehydrogenase is a 100-kDa dimer composed of 51-kDa subunits, prefers NADP+ as coenzyme, and preferentially oxidizes benzaldehyde-like aromatic aldehydes as well as medium chain length (4-9 carbons) aliphatic aldehydes. The substrate and coenzyme specificity, immunochemical properties, effect of disulfiram, pH profile, and isoelectric point of cornea aldehyde dehydrogenase are identical to those of tumor-associated aldehyde dehydrogenase, the prototype class 3 enzyme. The substrate and coenzyme preferences are consistent with a role for cornea aldehyde dehydrogenase in the oxidation of a variety of aldehydes generated by lipid metabolism, including lipid peroxidation.
醛脱氢酶已通过一步法从大鼠角膜中纯化出来。该酶属于3类醛脱氢酶。角膜醛脱氢酶是一种由51 kDa亚基组成的100 kDa二聚体，更喜欢NADP⁺作为辅酶，并优先氧化苯甲醛样芳香醛以及中链长度（4 - 9个碳）的脂肪醛。角膜醛脱氢酶的底物和辅酶特异性、免疫化学性质、双硫仑的作用、pH曲线以及等电点与肿瘤相关醛脱氢酶（3类酶的原型）相同。底物和辅酶偏好与角膜醛脱氢酶在氧化脂质代谢产生的多种醛（包括脂质过氧化）中的作用一致。
