Results 211 to 220 of about 43,981 (239)
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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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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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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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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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Immobilization of polynucleotide phosphorylase on inorganic support

Journal of Fermentation Technology, 1986
Abstract Polynucleotide phosphorylase was immobilized on aminopropyl porous glass by various covalent binding methods. The enzyme immobilized with glutaraldehyde exhibited the highest activity and had the same optimal pH as the free enzyme. The specific activity of the immobilized enzyme was increased by treatment with SH-reducing agent.
Hiroshi Yamauchi   +3 more
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Polynucleotide Phosphorylase Is Required for Escherichia coli O157:H7 Growth Above Refrigerated Temperature

, 2014
Background: The growth of Escherichia coli O157:H7 in contaminated dairy and other refrigerated food products due to temperature fluctuation poses a major food safety threat. Effective control or inhibition of E.
Hujia   +3 more
semanticscholar   +1 more source

Polynucleotide phosphorylase and the archaeal exosome as poly(A)-polymerases

Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, 2008
The addition of poly(A)-tails to RNA is a phenomenon common to almost all organisms. Not only homopolymeric poly(A)-tails, comprised exclusively of adenosines, but also heteropolymeric poly(A)-rich extensions, which include the other three nucleotides as well, have been observed in bacteria, archaea, chloroplasts, and human cells.
Gadi Schuster   +4 more
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