• Journal of Microbiology
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• v.37 no.4
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• pp.218-223
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• 1999

Legionella pneumophila, the cause of Legionnaires disease, is able to survive intracellularly in eukaryotic cells such as monocytes, macrophages, and protozoan organisms. During protein biosynthesis, the rph gene encodes ribonuclease (RNase) PH which functions as a phosphorolytic nuclease that removes nucleotides following the CCA terminus of tRNA and as a nucleotidyl-transferase which adds nucleotides to the ends of RNA molecules by usingnucelside diohosphates as substrates. In this sutdy, the rph gene was screened in pUC19 library employing a DNA probe which was constructed from PCR based on a consensus pattern of multiple alignment of RNas PH. The encoded protein consists of 235 amino acid residues with a calculated molecular weight of 26,112 Daltons. The RNase PH signature domains are completely conserved.

• Bulletin of the Korean Chemical Society
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• v.31 no.7
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• pp.2081-2084
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• 2010

• Microbiology and Biotechnology Letters
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• v.8 no.1
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• pp.1-8
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• 1980

Changes of nucleic acid related substances and their enzymes during rice makkulli koji making were observed and enzymological properties of crude enzymes were examined. The results obtained were as follows : (1) The amounst of acid soluble phosphorus were increased, while no remarkable changes were observed in the component of total phosphorus during koji making. (2) AMP and IMP were increased, while ADP and ATP were decreased gradually in the course of process. (3) Activities of nucleic acid degrading enzymes were increased with the lapse of time. (4) In the crude enzyme solution extracted from rice makkulli koji, the optimal pH of RNase was 4.0~5.0 and those of PDase PNase were 5.0. (5) RNase and PMase were stable at the range of pH 4.0~5.0 and PDase was stable at the pH 4.0. (6) The optimal temperature of RNase was 55$^{\circ}C$, and that of PDase was at the range of 50~55$^{\circ}C$, and 5$0^{\circ}C$ for PMase. (7) Among the three enzymes, the heat stability was in order RNase, PDase and PMase, and especially PMase was so heat labile that it was almost inactivated at 7$0^{\circ}C$ for 10 min. (8) Inhibition by metal ions and other inhibitors was disclosed : C $u^{++}$ and Z $n^{++}$ inhibited the activity of RNase, and C $u^{++}$, NaF and N $a_2$HP $O_4$ inhibited that of PDase, while C $u^{++}$ and NaF inhibited the PMase activity.ctivity.