Results 111 to 120 of about 49,990 (134)
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The Journal of Biochemistry, 1978
We have detected in rat liver cytosol three enzymes (termed C-1, C-2, and C-3) which cleaved the RNA moiety of RNA-DNA hybrid. These enzymes were separated from each other by DEAE-Sephadex and Sephadex G-200 chromatography. C-1 and C-2 specifically act on the RNA moiety of RNA-DNA hybrid, while C-3 degrades single-stranded RNA as well as the RNA of the
Fumio Tashiro, Yoshio Ueno
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We have detected in rat liver cytosol three enzymes (termed C-1, C-2, and C-3) which cleaved the RNA moiety of RNA-DNA hybrid. These enzymes were separated from each other by DEAE-Sephadex and Sephadex G-200 chromatography. C-1 and C-2 specifically act on the RNA moiety of RNA-DNA hybrid, while C-3 degrades single-stranded RNA as well as the RNA of the
Fumio Tashiro, Yoshio Ueno
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Ribonuclease H evolution in retrotransposable elements
Cytogenetic and Genome Research, 2005Eukaryotic and prokaryotic genomes encode either Type I or Type II Ribonuclease H (RNH) which is important for processing RNA primers that prime DNA replication in almost all organisms. This review highlights the important role that Type I RNH plays in the life cycle of many retroelements, and its utility in tracing early events in retroelement ...
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Ribonuclease H activity in cultured plant cells
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1978Ribonuclease H (RNAase H) was extracted from cultured plant cells, strain GD-2 and characterized. RNAase H activity in logarithmical growing cells is much higher than that of stationary cells, and the response of RNAase H activity was very similar to that of DNA polymerase after culture.
Kinji Tsukada +2 more
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Ribonucleases H of retroviral and cellular origin
Pharmacology & Therapeutics, 1990Ribonucleases H (RNases H) are enzymes which catalyse the hydrolysis of the RNA-strand of an RNA-DNA hybrid. Retroviral reverse transcriptases possess RNase H activity in addition to their RNA- as well as DNA-dependent DNA-polymerizing activity. These enzymes transcribe the viral single stranded RNA-genome into double stranded DNA, which then can be ...
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Ribonuclease H activity in developing rat brain
Life Sciences, 1977Abstract A ribonucleolytic enzyme (RNase H) which degrades the RNA strand of a RNA-DNA double stranded hybrid has been extracted from rat brain and characterized. RNase H activity in the cerebella increased up to around 6th day after birth and then decreased in adult rat cerebella, just as DNA polymerase and DNA ligase.
Yoshio Sawasaki +2 more
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A capillary electrophoretic assay for ribonuclease H activity
Analytical Biochemistry, 2004A capillary electrophoretic assay was developed to measure the ribonuclease (RNase) H activity of human immunodeficiency virus (HIV) type 1 reverse transcriptase. Cleavage of a fluorescein-labeled RNA-DNA heteroduplex was monitored by capillary electrophoresis.
King C. Chan +9 more
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A Thermodynamic Comparison of Mesophilic and Thermophilic Ribonucleases H
Biochemistry, 1999The mechanisms by which thermophilic proteins attain their increased thermostability remain unclear, as usually the sequence and structure of these proteins are very similar to those of their mesophilic homologues. To gain insight into the basis of thermostability, we have determined protein stability curves describing the temperature dependence of the
Julie Hollien, Susan Marqusee
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Thermal and mechanical multistate folding of ribonuclease H
The Journal of Chemical Physics, 2009Two different classes of experimental techniques exist by which protein folding mechanisms are ascertained. The first class, of which circular dichroism is an example, probes thermally-induced folding. The second class, which includes atomic force microscopy and optical tweezers, measures mechanically-induced folding. In this article, we investigate if
Thomas A. Knotts +2 more
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The Journal of Biochemistry, 1981
Rat liver nuclei were isolated in aqueous solutions of low ionic strength or anhydrous glycerol. The presence of ribonuclease H (RNase H) [EC 3.1.4.34] activity in the cytoplasm is due to extraction of the nuclear enzyme by buffer and inorganic salts.
Kinji Tsukada +4 more
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Rat liver nuclei were isolated in aqueous solutions of low ionic strength or anhydrous glycerol. The presence of ribonuclease H (RNase H) [EC 3.1.4.34] activity in the cytoplasm is due to extraction of the nuclear enzyme by buffer and inorganic salts.
Kinji Tsukada +4 more
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Small molecule inhibitors of HIV RT Ribonuclease H
Bioorganic & Medicinal Chemistry Letters, 2010Two classes of compounds, thiocarbamates 1 and triazoles 2, have been identified as HIV RT RNase H inhibitors using a novel FRET-based HTS assay. The potent analogs in each series exhibited selectivity and were active in cell-based assays. In addition, saturable, 1:1 stoichiometric binding to target was established and time of addition studies were ...
Martin Di Grandi +9 more
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