Abstract:A nuclease with 3'-nucleotidase activity was purifed at least 2,500-fold from Tradescantia paludosa leaves by a process that included chromatography on Concanavalin A-Sepharose. The preparation contains several active isozymes without impurities as judged by gel electrophoresis, but immunological tests revealed one or two mJor and a few minor inactive components. Phosphatase, phosphodiesterase and 5'-nucleotidase were absent or minimal, as were the known glycoproteins, peroxidase and esterase. The nuclease was… Show more
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