• Journal of Animal Science and Technology
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• v.59 no.9
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• pp.20.1-20.9
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• 2017

Background: Ribonuclease (RNase) is one of the few toxic proteins that are present constantly in snake venoms of all types. However, to date this RNase is still poorly studied in comparison not only with other toxic proteins of snake venom, but also with the enzymes of RNase group. The objective of this paper was to investigate some properties of RNase from venom of Vietnam cobra Naja atra. Methods: Kinetic methods and gel filtration chromatography were used to investigate RNase from venom of Vietnam cobra. Results: RNase from venom of Vietnam cobra Naja atra has some characteristic properties. This RNase is a thermostable enzyme and has high conformational stability. This is the only acidic enzyme of the RNase A superfamily exhibiting a high catalytic activity in the pH range of 1-4, with $pH_{opt}=2.58{\pm}0.35$. Its activity is considerably reduced with increasing ionic strength of reaction mixture. Venom proteins are separated by gel filtration into four peaks with ribonucleolytic activity, which is abnormally distributed among the isoforms: only a small part of the RNase activity is present in fractions of proteins with molecular weights of 12-15 kDa and more than 30 kDa, but most of the enzyme activity is detected in fractions of polypeptides, having molecular weights of less than 9 kDa, that is unexpected. Conclusions: RNase from the venom of Vietnam cobra is a unique member of RNase A superfamily according to its acidic optimum pH ($pH_{opt}=2.58{\pm}0.35$) and extremely low molecular weights of its major isoforms (approximately 8.95 kDa for RNase III and 5.93 kDa for RNase IV).

• Bulletin of the Korean Chemical Society
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• v.29 no.5
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• pp.1063-1064
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• 2008

• Applied Biological Chemistry
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• v.20 no.2
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• pp.242-246
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• 1977

In the barly coleptile sections treated with either $1{\times}10^{-5}M$ abscisic acid (ABA) or $1{\times}10^{-5}M$ gibberellic acid (GA), the time course changes of ribonuclease (RNase) activity and ribonucleic acid (RNA) profiles were studied. The results may be summarized as follows: 1. While GA suppressed RNase activity, ABA activated it. 2. High level of s-RNA and low level of r-RNA compared with normal plant sections in hormone-untreated coleoptiles seemed to be the results of increased RNase activity in the incubation period. 3. While GA retarded the decomposition of r-RNA, ABA activated it and the results seemed to be related with RNase activity. 4. GA activated the synthesis of RNA-DNA component, and ABA suppressed it. 5. Increase in the amount of s-RNA with the treatment of ABA may be due to the decomposition of r-RNA.

• The Korean Journal of Mycology
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• v.14 no.3
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• pp.201-207
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• 1986

In order to study subcellular locality and characteristics of ribonuclease in Saccharomyces uvarum, subcelllar fractions $45,000{\times}g$ pellet fraction, post ribosomal fraction and ribosome fraction were extracted during late log, stationary phase and sugar starvation conditions. Ribonuclease activity was significantly increased in ribosomal fraction under stationary and sugar starvation conditions. Ribosomal ribonuclease was extracted by EDTA plus streptomycin sulfate and ammonium sulfate precipitation. The amount of ribosome in stationary and sugar starvation condition was decreased three to six fold as compared to that in the early log phase. The end products of ribosomal ribonuclease were detected by thin layer chromatography. It is postulated that the increase of ribosomal ribonuclease activity under sugar starvation results from 5'-rRNase, while the increase of rRNase activity under stationary phase results from 3'-rRNase.

• Horticultural Science & Technology
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• v.34 no.3
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• pp.453-460
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• 2016

The parentage of the horticulturally important pear cultivar 'Niitaka' was confirmed by determining its S-genotypes based on the S-RNase and $PpSFBB^{-{\gamma}}$ genes, and genotyping using simple sequence repeat (SSR) markers. Previous reports suggested that the cultivars 'Amanogawa' and 'Imamuraaki' were the parents of 'Niitaka', although the cultivars 'Chojuro' and 'Shinchu' were also examined as candidate parents, along with two other cultivars. In the present study, the S-genotype of 'Niitaka' was determined to be $S^3S^9$. The $S^9$-RNase of 'Niitaka' was found to be likely inherited from the parent 'Amanogawa' ($S^1S^9$) and the $S^3$-RNase from 'Chojuro' ($S^3S^5$) or 'Shinchu' ($S^3S^5$). Based on the S-genotypes, the cultivar 'Imamuraaki' ($S^1S^6$) had no contribution to the parentage of 'Niitaka' ($S^3S^9$). A total of 67 polymorphic SSR markers were used to further confirm the parentage of 'Niitaka'. Discrepancies were found at several SSR loci between 'Niitaka' and the cultivars 'Imamuraaki' and 'Shinchu', whereas 'Niitaka' inherited alleles from 'Amanogawa' and 'Chojuro' at all SSR loci. Therefore, our findings established that 'Amanogawa' and 'Chojuro' are the parents of pear cultivar 'Niitaka', and not 'Imamuraaki' as previously reported.

• Asian-Australasian Journal of Animal Sciences
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• v.3 no.2
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• pp.115-120
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• 1990

Extracellular nuclease(s) in buffalo rumen fluid were purified from strained rumen fluid by a procedure involving Seitz filtration, acetone fractionation and gel filtration on Sephadex G-100. The enzyme resolved into two peaks exhibiting both DNase and RNase activities. The molecular weight of enzyme corresponding to peaks I and II were approximately 30,000 and 12,000 respectively. The properties of enzymes from the two peaks, however, were same. Optimum temperature for both DNase and RNase activities was at $50^{\circ}C$. Whereas DNase activity was stable upto $60^{\circ}C$, RNase activity was stable only up to $50^{\circ}C$. DNase activity recorded two pH optima, one at pH 5.5 and the other at pH 7.0. RNase activity recorded a broad pH optimum between pH 6.0-8.0. pH stability of the enzyme coincided with pH optima for both the activities. DNase activity was stimulated by $Mg^{2+}$ and $Mn^{2+}$ and inhibited by $Fe^{2+}$, $Zn^{2+}$, $Hg^{2+}$ and $Ag^+$. RNase activity was also stimulated by $Mg^{2+}$ and $Mn^{2+}$ and inhibited by $Cu^{2+}$, $Fe^{2+}$, $Zn^{2+}$, $Hg^{2+}$ and $Ag^+$. Reducing agents stimulated both the activities.

• Animal cells and systems
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• v.2 no.4
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• pp.529-538
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• 1998

In order to analyze the intracellu1ar localization of specific RNA components of ribonucleoproteins (RNP) in Xenopus oocytes, a modified protocol of whole-mount in situ Hybridization is presented in this paper, Mitochondria specific 12S rRNA probe was used to detect the amplification and distribution of mitochondria in various stages of the oocyte life cycle, and the results were found to be consistent with previously known distribution of mitochondria. The results with other specific probes (U1 and U3 small nuclear RNAs, and 5S RNA) also indicate that this procedure is generally effective in localizing RNAs in RNP complexes even inside organelles. In addition, the RNA component of RNase MRP, the RNP with endoribo-nuclease activity, localize to the nucleus in various stages of the oocyte life cycle. Some of MRP RNA, however, were found to be localized to the special population of mitochondria near the nucleus, especially in the active stage of mitochondrial amplification. It suggests dual localization of RNase MRP in the nucleus and mitochondria, which is consistent with the proposed roles of RNase MRP in mitochondrial DNA replication and in rRNA processing in the nucleolus.

• Bulletin of the Korean Chemical Society
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• v.32 no.6
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• pp.2137-2138
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• 2011

• Bulletin of the Korean Chemical Society
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• v.29 no.10
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• pp.2026-2028
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• 2008

• Bulletin of the Korean Chemical Society
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• v.30 no.5
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• pp.1193-1194
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• 2009