Literature DB >> 4308330

The influence of the size and nature of basic activators on Clostridium perfringens polynucleotide phosphorylase-catalysed polyadenylic acid synthesis.

P S Fitt, H Wille.   

Abstract

1. Basic oligo- and poly-(amino acids) stimulate polyadenylic acid synthesis by purified Clostridium perfringens polynucleotide phosphorylase (nucleoside diphosphate-polyribonucleotide nucleotidyltransferase, EC 2.7.7.8). 2. The effectiveness of the activators increases with chain length up to approx. 20-30 residues. 3. Polymers of the l and dl series are equally effective on a weight-for-weight basis. 4. l-Lysine, d-lysine, diethylamine and triethylamine, as hydrochlorides or hydrobromides, all stimulate the reaction markedly if their concentration is high enough. Their effect is similar to that of sodium chloride. 5. The size of the product depends primarily on the Mg(2+) concentration and basic polymers have a relatively limited effect on it. 6. Polyadenylic acid itself undergoes an Mg(2+)-catalysed non-enzymic hydrolysis.

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Year:  1969        PMID: 4308330      PMCID: PMC1187738          DOI: 10.1042/bj1120497

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  6 in total

1.  [Behavior and specificity of cerium and lanthanum as phosphatase models in the dephosphorylation of nucleic acids and mononucleotides].

Authors:  E BAMANN; H TRAPMANN; F FISCHLER
Journal:  Biochem Z       Date:  1954

2.  [The behavior and specificity of cerium, lanthanum, iron and aluminum as phosphatase models against physiologically important phosphoric acid compounds such as sugar phosphates, adenylic acid, adenosinetriphosphoric acids and others].

Authors:  E BAMANN; F FISCHLER; H TRAPMANN
Journal:  Biochem Z       Date:  1954

3.  The preferential loss of the polylysine- or polyornithine-stimulated activity of Clostridium perfringens polynucleotide phosphorylase during proteolysis.

Authors:  P S Fitt; H Wille
Journal:  Biochem J       Date:  1969-05       Impact factor: 3.857

4.  Protein-nucleic acid interaction. I. Nuclease-resistant polylysine-ribonculeic acid complexes.

Authors:  H A Sober; S F Schlossman; A Yaron; G W Latt SA RUSHIZKY
Journal:  Biochemistry       Date:  1966-11       Impact factor: 3.162

5.  A study by polyacrylamide-gel electrophoresis of the effect of proteolysis on Micrococcus lysodeikticus polynucleotide phosphorylase.

Authors:  P S Fitt; E A Fitt; H Wille
Journal:  Biochem J       Date:  1968-12       Impact factor: 3.857

6.  Irreversible heat inactivation of transfer ribonucleic acids.

Authors:  T Lindahl
Journal:  J Biol Chem       Date:  1967-04-25       Impact factor: 5.157

  6 in total
  4 in total

1.  The preferential loss of the polylysine- or polyornithine-stimulated activity of Clostridium perfringens polynucleotide phosphorylase during proteolysis.

Authors:  P S Fitt; H Wille
Journal:  Biochem J       Date:  1969-05       Impact factor: 3.857

2.  Partial purification and properties of guinea-pig liver polynucleotide phosphorylase.

Authors:  Y P See; P S Fitt
Journal:  Biochem J       Date:  1970-09       Impact factor: 3.857

3.  A study of the localization of polynucleotide phosphorylase within rat liver cells and of its distribution among rat tissues and diverse animal species.

Authors:  Y P See; P S Fitt
Journal:  Biochem J       Date:  1972-11       Impact factor: 3.857

4.  Partial purification and properties of rat liver mitochondrial polynucleotide phosphorylase.

Authors:  Y P See; P S Fitt
Journal:  Biochem J       Date:  1972-11       Impact factor: 3.857

  4 in total

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