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Studies of the activity of subunits of aspartate 4-decarboxylase immobilized on sepharose.

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