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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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 5:47 a.m.) |
Deposited | 1 year, 7 months ago (Jan. 10, 2024, 9:12 p.m.) |
Indexed | 1 year, 7 months ago (Jan. 11, 2024, 10:20 a.m.) |
Issued | 61 years ago (Aug. 7, 1964) |
Published | 61 years ago (Aug. 7, 1964) |
Published Print | 61 years ago (Aug. 7, 1964) |
@article{Singer_1964, title={Specificity of Potassium-Activated Phosphodiesterase of Escherichia coli}, volume={145}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.145.3632.593}, DOI={10.1126/science.145.3632.593}, number={3632}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Singer, Maxine F. and Tolbert, George}, year={1964}, month=aug, pages={593–595} }