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Enzymic synthesis of polynucleotides I. polynucleotide phosphorylase of Azotobacter vinelandii
Biochimica et Biophysica Acta, 1956The 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.
M, GRUNBERG-MANAGO, P J, ORTIZ, S, OCHOA
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Model for the elongation of polynucleotide chains by polynucleotide phosphorylase
Journal of Molecular Biology, 1970Abstract The experiments described in this paper were designed to elucidate the mechanism of elongation of a polynucleotide chain catalysed by polynucleotide phosphorylase. The problem has been approached in three different ways, essentially: (1) examination of the size distribution of the end products isolated during the course of the reaction; (2 ...
M N, Thang +2 more
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17 Polynucleotide Phosphorylase
1982Publisher 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.
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18 Polynucleotide Phosphorylase
1972Publisher 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
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Activation of Polynucleotide Phosphorylase by Salts
Nature, 1957IN 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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THE MECHANISM OF ACTION OF POLYNUCLEOTIDE PHOSPHORYLASE
Annals of the New York Academy of Sciences, 1959The purpose of this paper is to review certain aspects of the mechanism of action of polynucleotide phosphorylase and to present, rather briefly, some recent findings. The discussion will be concerned with studies carried out by S. Ochoa and his associates a t New York University, New York, N.
L A, HEPPEL, M F, SINGER, R J, HILMOE
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Conserved domains in polynucleotide phosphorylase among eubacteria
Biochimie, 2005Polynucleotide phosphorylase (PNPase) is a polynucleotide nucleotidyl transferase (E. C. 2.7.7.8) that is involved in mRNA degradation in prokaryotes. PNPase structure analysis has been performed in Streptomyces antibioticus; this revealed the presence of five domains: two ribonuclease PH (RPH)-like (pnp1 and pnp2), one alpha helical, one KH, and one ...
Rosa María, Bermúdez-Cruz +4 more
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POLYNUCLEOTIDE PHOSPHORYLASE IN NEISSERIA MENINGITIDIS
Acta Pathologica Microbiologica Scandinavica, 1963S, JYSSUM, K, JYSSUM
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[Animal tissue polynucleotide phosphorylase].
Biokhimiia (Moscow, Russia), 1978Localization, physico-chemical and catalytic properties and possible biological functions of polynucleotide phosphorylase (PNPase) from animal tissues are discussed. In animal tissue cells PNPase has multiple localization; the major amount of the enzyme is localized in the endoplasmic reticulum ribosomes.
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