Multiple forms of rabbit intestinal adenosine deaminase. characterization of two molecular species

摘要: Abstract 1. Two forms of adenosine deaminase (adenosine amino-hydrolase, EC 3.5.4.4.). previously purified from rabbit intestine were shown to have similar isoelectric points and relative substrate specificities, but differed in their electrophoretic mobilities, activation energies, arnino acid compositions K m values. 2. Both the enzyme could be inactivated by p -chloromercuriphenylsulphonic acid, -chloro-mercuribenzoate phenylmercuriacetate, not inhibited iodoacetic or its amide. 3. The inactivation -chloromercuribenzoate reversed addition 2-mercaptoethanol dithiothreitol. 4. also Cu + , 2+ Ca urea. guanidine hydrochloride sodium sulphite. 5. Treatment large molecular with dodecyl sulphate resulted production 2 subunit species one which had same mobility mol. wt as small deaminase.