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dc.contributor.authorSharp, A.J.
dc.contributor.authorWalker, John
dc.identifier.citationSharp , A J & Walker , J 1993 , ' Mung-bean nuclease 1 (EC ' , Methods in Molecular Biology , vol. 16 , pp. 253-261 .
dc.identifier.otherPURE: 326942
dc.identifier.otherPURE UUID: da2be060-a67e-415a-a5cc-9856502b6b33
dc.identifier.otherScopus: 79959319436
dc.descriptionThe original publication is available at Copyright Humana Press [Full text of this article is not available in the UHRA]
dc.description.abstractMung-bean nuclease 1 was first purified by Sung and Laskowski (1) in 1962 from mung-bean sprouts (Phaseolus aureus). It belongs to the class of enzymes EC, which has a preference for single-stranded nucleic acid substrates, lacks sugar specificity, and hydrolyzes single-stranded substrates to produce products with 5-phoshoryl and 3-hydroxl termini, ranging fro mono-to, at least, heptanucleotides. Although it shows a preference for single-stranded nucleic acids over double-stranded of 30,000-fold (2), used in high concentrations with extended incubation times, mung-bean nuclease 1 will completely degrade double-stranded DNA (3-5). Mung-bean nuclease 1 is also reported to show a separate 3-(1)-monophosphatase activity (6). Mung-bean nuclease 1 is a zinc metalloenzyme that requires Zn2+ and a reducing agent, such as cysteine, for both activity and stability.en
dc.relation.ispartofMethods in Molecular Biology
dc.titleMung-bean nuclease 1 (EC
dc.contributor.institutionDepartment of Human and Environmental Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.description.statusPeer reviewed
rioxxterms.typeJournal Article/Review

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