Abstract
Gel filtration of human thyroid extract with Sephadex G-200 revealed two molecular forms of adenosine deaminase differing in their molecular sizes. The smaller form of adenosine deaminase was purified over 120-fold by precipitation of the protein impurities at pH5.6 and chromatogaphy on DEAE-Sephadex A-50, Sephadex G-100 and adenosine-Sepharose. The purified enzyme was specific towards adenosine. The Michaelis constant was 5.2 × 10 −5 M. The optimum pH was about 7.0 and molecular weight 42000.
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