title: Affinity difference of adenosine deaminases for the purine riboside-epoxyactivated Sepharose 6B column.
abstract: The small-size adenosine deaminase (Mr = 35,000 and 43,000) in calf intestinal mucosa, frog liver and scallop adductor muscle and the large-size deaminase (Mr = 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. Binding of the other large-size enzymes (Mr = 140,000) in the midgut gland of scallop and mussel to the column was not successful. 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.
mesh_terms: D000243:Adenosine Deaminase / Q000302:isolation & purification*; D000818:Animals; D049872:Bivalvia / Q000201:enzymology; D002417:Cattle; D002846:Chromatography, Affinity; D007413:Intestinal Mucosa / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D008970:Molecular Weight; D008974:Mollusca / Q000201:enzymology; D009700:Nucleoside Deaminases / Q000302:isolation & purification*; D011684:Purine Nucleosides; D011892:Rana catesbeiana; D012263:Ribonucleosides; D013045:Species Specificity
chemical_list: D011684:Purine Nucleosides; D012263:Ribonucleosides; C005248:nebularine; D009700:Nucleoside Deaminases; D000243:Adenosine Deaminase