Abstract
1. 1. The small-size adenosine deaminases ( M r = 35,000 and 43,000 ) in calf intestinal mucosa, frog liver and scallop adductor muscle and the large-size deaminase ( M r = 100,000 ) in frog liver probably formed by adding a conversion protein to the small enzyme, were tightly bound to the purine riboside affinity column. 2. 2. Binding of the other large-size enzymes ( M r = 140,000 ) in the midgut gland of scallop and mussel to the column was not successful. 3. 3. It seems that the binding difference does not depend on a change in affinity between active site and ligand but rather on the stereospecific positioning of active site in the enzyme molecules.
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