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Large-scale Production of Recombinant RNAs on a Circular Scaffold Using a Viroid-derived System in Escherichia coli
Published on: November 30, 2018
A ribonuclease with distinctive features from the wild green-headed mushroom Russulus virescens
1Department of Microbiology, College of Biological Science, China Agricultural University, and State Key Laboratory of Agrobiotechnology, Beijing, China.
Abstract:
A ribonuclease with an N-terminal sequence different from those of other ribonucleases has been purified from fruiting bodies of the mushroom Russula virescens. The RNase was adsorbed on DEAE-cellulose and Q-Sepharose in 10mM Tris-HCl buffer (pH 7.1-7.3) and on CM-Sepharose in 10mM NH(4)OAc buffer (pH 4.6), unlike other mushroom ribonucleases which are unadsorbed on DEAE-cellulose. The RNase demonstrated a molecular mass of 28kDa in both gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. In contrast to other mushroom ribonucleases which are monospecific, it exhibited co-specificity towards poly A and poly C. It demonstrated a pH optimum of 4.5, which is lower than values reported for other mushroom ribonucleases, and a temperature optimum of 60 degrees C.
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