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dc.contributor.authorSweeney, P.J.
dc.contributor.authorWalker, John
dc.date.accessioned2011-08-22T09:01:04Z
dc.date.available2011-08-22T09:01:04Z
dc.date.issued1993
dc.identifier.citationSweeney , P J & Walker , J 1993 , ' Proteinase K (EC 3.4.21.14) ' , Methods in Molecular Biology , vol. 16 , pp. 305-311 . https://doi.org/10.1385/0-89603-234-5:305
dc.identifier.issn1064-3745
dc.identifier.otherPURE: 326915
dc.identifier.otherPURE UUID: 0bd989c7-4b8e-46e2-b81e-a49f89d90454
dc.identifier.otherScopus: 79959308231
dc.identifier.urihttp://hdl.handle.net/2299/6324
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.abstractProteinase K is a serine protease and the main proteolytic enzyme produced by the fungus Tritirachium album Limber (l). The enzyme has a broad specificity, cleaving peptide bonds C-terminal to a number of amino acids. The enzyme is produced, together with other proteases and an aminopeptidase, during stationary phase when the fungus is grown by submerged culture. The enzyme is so named because the organism can grow on native keratin as sole carbohydrate and nitrogen source owing to the enzyme’s ability to digest keratin. Because of its broad substrate specificity, high activity, and its ability to digest native proteins, proteinase K has found considerable use in procedures where the inactivation and degradation of proteins is required, particularly during the purification of nucleic acids.en
dc.language.isoeng
dc.relation.ispartofMethods in Molecular Biology
dc.titleProteinase K (EC 3.4.21.14)en
dc.contributor.institutionDepartment of Human and Environmental Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.description.statusPeer reviewed
rioxxterms.versionofrecordhttps://doi.org/10.1385/0-89603-234-5:305
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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