Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.27.4 (ribonuclease)
 6,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effectiveness of several commonly used inhibitors of ribonuclease (RNAase) has been studied using the removal of radio-labelled leucine from leucyl-tRNA as a sensitive assay for RNAase activity. The inhibitors were tested under a variety of conditions, varying the temperature, the pH, and the source of RNAase. When each inhibitor is udes separately in the presence of pancreatic RNAase, sodium dodecyl sulfate (SDS) is the most effective; but during long exposures to temperatures above 0 degrees C considerable amounts of RNA are still degraded. Combination of inhibitors are more effective in preserving RNA; with this assay, a combination of SDS with diethyl pyrocarbonate is the most effective. Proteinase K acts as an inhibitor when used in combination with SDS; however, it has RNAase activity when used by itself. Diethyl pyrocarbonate, when used at the high range of concentrations employed by others for RNAase inhibition, reacts with RNA changing its charge. However, when diethyl pyrocarbonate is used in smaller amounts the effects on RNA are minimal, and when used in combination with SDS it effectively inhibits RNAase.
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PMID:Inhibition of ribonuclease. Efficacy of sodium dodecyl sulfate, diethyl pyrocarbonate, protein ase K and heparin using a sensitive ribonuclease assay. 2 20

The nucleotide sequence of wheat (Triticum aestivum) 5.8-S ribosomal RNA has been re-examined using partial chemical degradation with high-temperature sequencing gels and oligonucleotide analysis. The results clarify previously ambiguous residues and add two additional nucleotides, G127 and G135, to the sequence. Estimates of the secondary structure suggest that 5.8-S rRNAs of higher plants differ from previous examples in having more open G + C-rich and A + U-rich stems. S1 ribonuclease digestion was used to probe this secondary structure; the data generally support the 'burp gun' model proposed for all 5.8-S rRNAs but are also consistent with a more open A + U-rich stem. Diethyl pyrocarbonate reactivity was used to probe the topography of this RNA in wheat ribosomes. The results indicate that the G + C-rich and A + U-rich stems are accessible to chemical modification in the wheat ribosome and suggest that the A + U-rich stem undergoes a significant conformational change when the molecule associates into ribosomes.
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PMID:Studies on the secondary structure of wheat 5.8 S rRNA. Conformational changes in the A + U-rich stem during ribosome assembly. 706 May 53