Ribonucleic acid (RNA) from torula yeast may be used as a substrate for studying ribonuclease activities of enzymes such as ribonuclease-A, ribonuclease T1 (RNAase) and bougainvillea xbuttiana antiviral protein 1 (BBAP1).
Ribonuclease (RNase), which often represents molecular biological contamination, is a thermostable enzyme. When RNase is heated at 121 degrees C by autoclave sterilization for 20 min, it does not lose its activity. However, the nature of the molecular events by
Three nucleosides catalyzing the oxidoreduction of NADH and K3Fe(CN)6 were isolated from Torula yeast RNA and also obtained by a series of steps: SDS-phenol extraction, nuclease P1 digestion, alkaline phosphatase digestion, anion exchange chromatography, and HPLC on an ODS column.
We report on the effect of the viscogenic agents glycerol and ficoll on the RNase T1 catalyzed turnover of GpA, GpC, GpU, and Torula yeast RNA. For wild-type enzyme, we find that the kcat/Km values for the transesterification of GpC
Nucleic acids research, 41(Web Server issue), W492-W498 (2013-06-14)
To facilitate the analysis of large-scale high-throughput capillary electrophoresis data, we previously proposed a suite of efficient analysis software named HiTRACE (High Throughput Robust Analysis of Capillary Electrophoresis). HiTRACE has been used extensively for quantitating data from RNA and DNA
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