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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

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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860
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40.54
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28
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References
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Journal of Biological Chemistry · 1951 · 317,666 citations
A quantitative assay for DNA-RNA hybrids with DNA immobilized on a membrane
Journal of Molecular Biology · 1965 · 1,971 citations
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