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dc.contributor.authorSharp, A.J.
dc.contributor.authorWalker, John
dc.date.accessioned2011-08-22T09:01:05Z
dc.date.available2011-08-22T09:01:05Z
dc.date.issued1993
dc.identifier.citationSharp , A J & Walker , J 1993 , ' Mung-bean nuclease 1 (EC 3.1.30.1) ' , Methods in Molecular Biology , vol. 16 , pp. 253-261 . https://doi.org/10.1385/0-89603-234-5:253
dc.identifier.issn1064-3745
dc.identifier.otherPURE: 326942
dc.identifier.otherPURE UUID: da2be060-a67e-415a-a5cc-9856502b6b33
dc.identifier.otherScopus: 79959319436
dc.identifier.urihttp://hdl.handle.net/2299/6325
dc.descriptionThe original publication is available at www.springerlink.com 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 3.1.30.1., 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.language.isoeng
dc.relation.ispartofMethods in Molecular Biology
dc.titleMung-bean nuclease 1 (EC 3.1.30.1)en
dc.contributor.institutionDepartment of Human and Environmental Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.description.statusPeer reviewed
rioxxterms.versionofrecordhttps://doi.org/10.1385/0-89603-234-5:253
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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