Studies of the activity of subunits of aspartate 4-decarboxylase immobilized on sepharose.
作者： Sei-ichiro IKEDA , Saburo FUKUI
DOI: 10.1111/J.1432-1033.1974.TB03649.X
关键词:
摘要: The relationship between the subunit structure and activity of aspartate 4-decarboxylase from Pseudomonas dacunhae was studied by immobilizing dissociated enzyme molecules on CNBr-activated Sepharose, thus preventing them reassociation. Sepharose-bound (half molecular weight native enzyme), which prepared in presence 1 M guanidine-HCl, showed a specific about 60% that for original undissociated bound Sepharose. immobilized confirmed means dissociation procedure treated with or 5 guanidine-HCl. Reassociation hybrid formation experiments also supported idea is higher than activity. 2-Oxoglutarate activated both enzymes to same extent as soluble enzyme. affinity substrate altered somewhat immobilization, but hardly influenced
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