Literature DB >> 14163788

SPECIFICITY OF POTASSIUM-ACTIVATED PHOSPHODIESTERASE OF ESCHERICHIA COLI.

M F SINGER, G TOLBERT.   

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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Keywords:  ADENINE NUCLEOTIDES; CARBON ISOTOPES; CHROMATOGRAPHY; ESCHERICHIA COLI; EXPERIMENTAL LAB STUDY; NUCLEOTIDASES; POLYNUCLEOTIDES; POTASSIUM; URACIL NUCLEOTIDES

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Year:  1964        PMID: 14163788     DOI: 10.1126/science.145.3632.593

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  2 in total

1.  Multiple determinants of functional mRNA stability: sequence alterations at either end of the lacZ gene affect the rate of mRNA inactivation.

Authors:  C Petersen
Journal:  J Bacteriol       Date:  1991-04       Impact factor: 3.490

Review 2.  RNA precursor molecules and ribonucleases in E. coli.

Authors:  S Altman; H D Robertson
Journal:  Mol Cell Biochem       Date:  1973-05-11       Impact factor: 3.396

  2 in total

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