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Purification and Further Properties of Single‐Strand‐Specific Nuclease from <i>Aspergillus oryzae</i>
European Journal of Biochemistry · 1973 · Vol. 33(1) · pp. 192–200
Volker M. Vogt✉(Swiss Cancer Center Léman)
Abstract
A simple scheme has been devised for the purification of Aspergillus nuclease S 1 from commercially available crude amylase powder. Five purification steps yield 90% pure nuclease with an overall yield of 27%. The enzyme is shown to be absolutely specific for single‐stranded nucleic acids. It degrades both DNA and RNA. The nuclease exhibits a sharp pH optimum at pH 4.2 and is active in low concentrations of dodecylsulfate. Aspergillus nuclease S 1 is a metalloprotein of molecular weight 32000. The utility of this nuclease for measuring annealing of labeled DNA is discussed.
Advanced biosensing and bioanalysis techniquesCRISPR and Genetic EngineeringDNA and Nucleic Acid ChemistryNucleaseAspergillus oryzaeNucleic acidDNARNAChemistryEnzymeAspergillus nigerBiochemistryAspergillus
MeSH terms
AmylasesAspergillusChromatography, DEAE-CelluloseDeoxyribonucleasesDNA, Single-StrandedHydrogen-Ion ConcentrationMetalloproteinsMolecular WeightNucleic Acid HybridizationRibonucleasesSodium Dodecyl Sulfate
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28
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References
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Journal of Biological Chemistry · 1969 · 20,334 citations
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Journal of Biological Chemistry · 1951 · 317,666 citations
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Journal of Molecular Biology · 1965 · 1,971 citations
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