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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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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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Inhibitory Action of Tetracyclines on Polynucleotide Phosphorylase*
The Journal of Biochemistry, 1966Jun Okuda, Ichiro Fuwa
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