Results 201 to 210 of about 40,696 (222)
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Immobilization of polynucleotide phosphorylase on inorganic support
Journal of Fermentation Technology, 1986Abstract 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 and the archaeal exosome as poly(A)-polymerases
Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, 2008The 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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, 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
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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
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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Archives of Biochemistry and Biophysics, 1958
Abstract The rate of synthesis of polyadenylic acid by the polynucleotide phosphorylase enzyme system of M. lysodeikticus is increased by the addition of salts. The activation by salts results from a decrease in K m ; V m is unaltered. In contrast, Mg increases both K m and V m to a comparable degree.
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Abstract The rate of synthesis of polyadenylic acid by the polynucleotide phosphorylase enzyme system of M. lysodeikticus is increased by the addition of salts. The activation by salts results from a decrease in K m ; V m is unaltered. In contrast, Mg increases both K m and V m to a comparable degree.
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POLYNUCLEOTIDE PHOSPHORYLASE IN NEISSERIA MENINGITIDIS
Acta Pathologica Microbiologica Scandinavica, 1963Kaare Jyssum, Sidsel Jyssum
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