BOVINE CORNEAL ALDEHYDE DEHYDROGENASE - THE MAJOR SOLUBLE CORNEAL PROTEIN WITH A POSSIBLE DUAL PROTECTIVE ROLE FOR THE EYE
BOVINE CORNEAL ALDEHYDE DEHYDROGENASE - THE MAJOR SOLUBLE CORNEAL PROTEIN WITH A POSSIBLE DUAL PROTECTIVE ROLE FOR THE EYE
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DOI：
10.1016/0014-4835(90)90154-m
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发表时间：
1990-10-01
影响因子：
3.4
通讯作者：
HOLMES, RS
中科院分区：
文献类型：
--
作者：
ABEDINIA, M;PAIN, T;HOLMES, RS
将牛角膜醛脱氢酶纯化至均一，并在pH 7.4下用醛底物进行表征。该酶是一种二聚体，亚基大小为65 kDa。使用kcat/Km值作为底物功效的指示，脂质过氧化的醛产物被认为是可能的“天然"底物。从酶纯化的蛋白质产量，以及粗和纯化的酶制剂的电泳分析，表明这种酶是牛角膜中的主要可溶性蛋白质，并构成约0.5%的组织湿重。本文提出了ALDH在保护眼睛免受UV-B光伤害中的双重作用，即光诱导的脂质过氧化作用产生的醛的氧化作用和牛角膜ALDH对UV-B光的直接吸收。
Bovine corneal aldehyde dehydrogenase was purified to homogeneity and characterized with aldehyde substrates at pH 7.4. The enzyme was a dimer with a subunit size of 65 kDa. Using kcat/Km values as an indication of substrate efficacy, aldehyde products of lipid peroxidation were recognized as the likely ''natural'' substrates. Protein yields from enzyme purification, as well as electrophoretic analyses of crude and purified enzyme preparations, demonstrated that this enzyme is the major soluble protein in bovine cornea, and constitutes around 0.5% wet weight of tissue. A dual role in protecting the eye against UV-B light is proposed.sbd.oxidation of aldehyde generated by light induced lipid peroxidation, and the direct absorption of UV-B light by bovine corneal ALDH.