Crossref journal-article
American Association for the Advancement of Science (AAAS)
Science (221)
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.

Bibliography

Singer, M. F., & Tolbert, G. (1964). Specificity of Potassium-Activated Phosphodiesterase of Escherichia coli. Science, 145(3632), 593–595.

Authors 2
  1. Maxine F. Singer (first)
  2. George Tolbert (additional)
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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)
Funders 0

None

@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} }