King G, Holmes R S
School of Science, Griffith University, Nathan, Brisbane, Australia.
Biochem Mol Biol Int. 1993 Sep;31(1):49-63.
Human corneal aldehyde dehydrogenase (designated ALDH3) was purified to homogeneity and characterised with respect to substrate specificity and inhibition by thiol reagents. The enzyme was present as a major soluble protein (5% of the total soluble protein) and was found to efficiently catalyse the oxidation of medium chain peroxidic aldehydes which may be found in the cornea. These findings are consistent with the proposal that ALDH3 plays a dual role in the absorption of UVR and in the oxidation of peroxidic aldehydes in the mammalian cornea. Disulfiram did not inhibit this enzyme under the conditions used in this study, however p-hydroxymercuribenzoate rapidly inactivated the enzyme. Analysis of the proteins of the cornea and surrounding tissue indicated that in both the cow and the human, changes in the nature and quantity of soluble proteins occurred. Phenotype variants of the ALDH3 were apparent in a small Australian population.
人角膜醛脱氢酶（命名为ALDH3）被纯化至同质，并就底物特异性和硫醇试剂的抑制作用进行了表征。该酶作为一种主要的可溶性蛋白质存在（占总可溶性蛋白质的5%），并被发现能有效催化角膜中可能存在的中链过氧化物醛的氧化。这些发现与ALDH3在哺乳动物角膜中紫外线吸收和过氧化物醛氧化中起双重作用的提议一致。在本研究使用的条件下，双硫仑不抑制该酶，然而对羟基汞苯甲酸迅速使该酶失活。对角膜和周围组织的蛋白质分析表明，在牛和人中，可溶性蛋白质的性质和数量都发生了变化。ALDH3的表型变异在一小部分澳大利亚人群中很明显。
