ArticleNucleic acids research1992
A pyrimidine-guanine sequence-specific ribonuclease from Rana catesbeiana (bullfrog) oocytes.
Article in Nucleic acids research, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 43 citations in OpenAlex.
- Discovery of antitumor effects of leczymes.Glycoconjugate journal · 2022Review
- Evolutionary Trends in RNA Base Selectivity Within the RNase A Superfamily.Frontiers in pharmacology · 2019Article
- Sialic Acid-Binding Lectin from Bullfrog Eggs Exhibits an Anti-Tumor Effect Against Breast Cancer Cells Including Triple-Negative Phenotype Cells.Molecules (Basel, Switzerland) · 2018Article
- Sialic acid-binding lectin from bullfrog eggs inhibits human malignant mesothelioma cell growth in vitro and in vivo.PloS one · 2018Article
- RNase activity of sialic acid-binding lectin from bullfrog eggs drives antitumor effect via the activation of p38 MAPK to caspase-3/7 signaling pathway in human breast cancer cells.International journal of oncology · 2016Article
- Sialyl-glycoconjugates in cholesterol-rich microdomains of P388 cells are the triggers for apoptosis induced by Rana catesbeiana oocyte ribonuclease.Glycoconjugate journal · 2014Article
- Cancer-selective induction of apoptosis by leczyme.Frontiers in oncology · 2014Review
- Sialic acid-binding lectin (leczyme) induces caspase-dependent apoptosis-mediated mitochondrial perturbation in Jurkat cells.International journal of oncology · 2013Article
- Evasion of ribonuclease inhibitor as a determinant of ribonuclease cytotoxicity.Current pharmaceutical biotechnology · 2008Review
- RNase T1 mimicking artificial ribonuclease.Nucleic acids research · 2007Article
- The structural integrity exerted by N-terminal pyroglutamate is crucial for the cytotoxicity of frog ribonuclease from Rana pipiens.Nucleic acids research · 2003Article
- 1H, 15N and 13C resonance assignments and secondary structure determination of the RC-RNase 2 from oocytes of bullfrog Rana catesbeiana.Journal of biomolecular NMR · 2001Article
- Purification and cloning of cytotoxic ribonucleases from Rana catesbeiana (bullfrog).Nucleic acids research · 2000Article
- The secondary structure of a pyrimidine-guanine sequence-specific ribonuclease possessing cytotoxic activity from the oocytes of Rana catesbeiana.Journal of biomolecular NMR · 1996Article
- Immunocytochemical localization of ribonuclease in yolk granules of adult Rana catesbeiana oocytes.Cell and tissue research · 1995Article
- Determination of base specificity of multiple ribonucleases from crude samples.Molecular biology reportsArticle
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A pyrimidine-guanine sequence-specific ribonuclease (RC-RNase) was purified from Rana catesbeiana (bullfrog) oocytes by sequential phosphocellulose, Sephadex G75, heparin Sepharose CL 6B and CM-Sepharose CL 6B column chromatography. The purified enzyme with molecular weight of 13,000 daltons gave a single band on SDS-polyacrylamide gel. One CNBr-cleaved fragment has a sequence of NVLSTTRFQLNT/TRTSITPR, which is identical to residues 59-79 of a sialic acid binding lectin from R. catesbeiana eggs, and is 71% homologous to residues 60-80 of an RNase from R. catesbeaina liver. The RC-RNase preferentially cleaved RNA at pyrimidine residues with a 3' flanking guanine under various conditions. The sequence specificity of RC-RNase was further confirmed with dinucleotide as substrates, which were analyzed by thin layer chromatography after enzyme digestion. The values of kcat/km for pCpG, pUpG and pUpU were 2.66 x 10(7) M-1s-1, 2.50 x 10(7) M-1s-1 and 2.44 x 10(6) M-1s-1 respectively, however, those for other phosphorylated dinucleotides were less than 2% of pCpG and pUpG. As compared to single strand RNA, double strand RNA was relatively resistant to RC-RNase. Besides poly (A) and poly (G), most of synthetic homo- and heteropolynucleotides were also susceptible to RC-RNase. The RC-RNase was stable in the acidic (pH 2) and alkaline (pH 12) condition, but could be inactivated by heating to 80 degrees C for 15 min. No divalent cation was required for its activity. Furthermore, the enzyme activity could be enhanced by 2 M urea, and inhibited to 50% by 0.12 M NaCl or 0.02% SDS.
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