Results 191 to 200 of about 40,696 (222)
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17 Polynucleotide Phosphorylase

1982
Publisher Summary Polynucleotide phosphorylase (PNPase) is the first enzyme that can catalyze the formation of polyribonucleotides with a 3′,5′-phosphodiester bond. In the forward reaction, long polyribonucleotides are synthesized from various ribonucleoside diphosphates, with elimination of inorganic orthophosphate.
H. Soreq, U.Z. Littauer
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18 Polynucleotide Phosphorylase

1972
Publisher Summary Polynucleotide phosphorylase (polyribonucleotide : orthophosphate nucleotidyltransferase) designated as PNPase was the first polynucleotide synthesizing enzyme to be discovered. It catalyzes the reversible polymerization of ribonucleoside diphosphates with release of inorganic phosphate. The product of PNPase synthesis is chemically
M. Grunberg-Manago, T. Godefroy-Colburn
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Synthesis of polypseudouridylic acid by polynucleotide phosphorylase

Biochimica et Biophysica Acta, 1963
Abstract 1. 1. Polypseudouridylic acid was synthesized in good yield from pseudouridine diphosphate by polynucleotide phosphorylase (EC 2.7.7.8) of Micrococcus lysodeikticus. Primer trinucleotide, pApApA markedly increased the synthetic reaction rate but did not affect the [32P]Pi-pseudouridine diphosphate exchange. 2. 2.
Irving H. Goldberg   +2 more
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Activation of Polynucleotide Phosphorylase by Salts

Nature, 1957
IN the course of purification studies of polynucleotide phosphorylase (polyase) from M. lysodeikticus we have on several occasions noticed that, after dialysis against buffers at low ionic strength or distilled water, considerable loss of enzyme activity occurred.
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Overexpression and purification of untagged polynucleotide phosphorylases

Protein Expression and Purification, 2003
We report here the development of new, straightforward procedures for the purification of bacterial polynucleotide phosphorylases (PNPases). The pnp genes from Streptomyces antibioticus, Streptomyces coelicolor, and Escherichia coli were overexpressed using the vectors pET11 and pET11A in E. coli BL21(DE3)pLysS.
Janet S. Hankins   +3 more
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Enzymic synthesis of polynucleotides I. polynucleotide phosphorylase of Azotobacter vinelandii

Biochimica et Biophysica Acta, 1956
The isolation, partial purification and some properties of polynucleotide phosphorylase of Azotobacter vinelandii are described. The enzyme catalyzes the synthesis of highly polymerized ribonucleic acid-like polynucleotides from 5′-nucleoside diphosphates with release of orthophosphate. The reaction requires magnesium ions and is reversible.
Marianne Grunberg-Manago   +2 more
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Human polynucleotide phosphorylase: location matters

Trends in Cell Biology, 2007
Human polynucleotide phosphorylase (hPNPase) is an RNA-processing enzyme induced in response to type I interferons and during terminal differentiation and cellular senescence. hPNPase was thought to contribute to cellular senescence through its RNA-degrading activity in the cytosol; however, recent studies show that hPNPase localizes to the ...
Carla M. Koehler   +2 more
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Polynucleotide phosphorylase from plant cells

Plant Cell Reports, 1984
The isolation of polynucleotide phosphorylase (EC 2. 7. 7. 8) from suspension cultured plant cells of parsley (Petroselinum sativum) and from tomato seedlings (Lycopersicon esculentum) is described. The procedure includes an ultracentrifugation step, a glycerol density gradient centrifugation and preparative gel electrophoresis under nondenaturing ...
Eva Schumacher-Wittkopf   +2 more
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Human Polynucleotide Phosphorylase, hPNPase, is Localized in Mitochondria

Journal of Molecular Biology, 2003
The human gene encoding a polynucleotide phosphorylase (hPNPase) has been recently identified as strongly up-regulated in two processes leading to irreversible arrest of cell division: progeroid senescence and terminal differentiation. Here, we demonstrate that the hPNPase is localized in mitochondria.
Piwowarski, Jan   +5 more
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Genetic analysis of polynucleotide phosphorylase structure and functions

Biochimie, 2007
Polynucleotide phosphorylase (PNPase) is a phosphate-dependent 3' to 5' exonuclease widely diffused among bacteria and eukaryotes. The enzyme, a homotrimer, can also be found associated with the endonuclease RNase E and other proteins in a heteromultimeric complex, the RNA degradosome.
Briani, F   +8 more
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