Specificity of Potassium-Activated Phosphodiesterase of Escherichia coli

Abstract
A potassium-activated phosphodiesterase that hydrolyzes polyribonucleotides to 5'-mononucleotides has been purified approximately 600-fold from extracts of Escherichia coli B. The purified enzyme appears to be specific for single-stranded polyribonucleotides: helical forms are not hydrolyzed, nor do they inhibit the hydrolysis of single-stranded chains.

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