[Isolation and some properties of exoribonuclease from the cell nuclei of the rat liver].
Biokhimiia, 1975/1-1975/2;40(1):13-20.
PMID: 237581
Abstract
Exoribonuclease from rat liver cell nuclei was isolated and purified using selective extraction at pH 8.0, salting out with ammonium sulfate (30-50% saturation) and chromatography on DEAE-Sephadex A-50. The enzyme has the pH optimum 7.4-7.6, it requires Mg-2+. It catalyses the gradual removal of ribonucleoside-5'-monophosphates from synthetic polynucleotides and RNA; it preferably attacks single-stranded polynucleotides and is less efficient when hydrolysing poly-stranded helical polymers. It is supposed that exoribonuclease can participate in the destruction of non-informative regions in new-formed hyper-molecular RNA of cell nuclei.
MeSH terms
Animals; Cell Fractionation; Cell Nucleus; Chromatography, DEAE-Cellulose; Chromatography, Gel; Chromatography, Thin Layer; Drug Stability; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Exonucleases; Hydrogen-Ion Concentration; Hydrolysis; Indicators and Reagents; Kinetics; Liver; Microscopy, Electron; Poly A-U; Poly U; Rats; Ribonucleases; Structure-Activity Relationship
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