绵羊肝线粒体醛脱氢酶的一些特性
Some properties of aldehyde dehydrogenase from sheep liver mitochondria.
作者信息
Hart G J, Dickinson F M
出版信息
Biochem J. 1977 May 1;163(2):261-7. doi: 10.1042/bj1630261.
Abstract
Aldehyde dehydrogenase from sheep liver mitochondria was purified to homogeneity as judged by electrophoresis on polyacrylamide gels, and by sedimentation-equilibrium experiments in the analytical ultracentrifuge. The enzyme has a molecular weight of 198000 and a subunit size of 48000, indicating that the molecule is a tetramer. Fluorescence and spectrophotometric titrations indicate that each subunit can bind 1 molecule of NADH. Enzymic activity is completely blocked by reaction of 4mol of 5,5'-dithiobis-(2-nitrobenzoate)/mol of enzyme. Excess of disulfiram or iodoacetamide decreases activity to only 50% of the control value, and only two thiol groups per molecule are apparently modified by these reagents.
摘要
通过聚丙烯酰胺凝胶电泳以及分析超速离心机中的沉降平衡实验判断，从绵羊肝脏线粒体中纯化得到的醛脱氢酶达到了均一性。该酶的分子量为198000，亚基大小为48000，表明该分子是一个四聚体。荧光和分光光度滴定表明每个亚基可以结合1分子NADH。每摩尔酶与4摩尔5,5'-二硫代双（2-硝基苯甲酸）反应会完全阻断酶活性。过量的双硫仑或碘乙酰胺会使活性仅降至对照值的50%，并且这些试剂显然仅修饰了每个分子中的两个巯基。
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