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Article: Ribonuclease U2: Cloning, production in Pichia pastoris and affinity chromatography purification of the active recombinant protein

TitleRibonuclease U2: Cloning, production in Pichia pastoris and affinity chromatography purification of the active recombinant protein
Authors
Issue Date2000
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journal.asp?ref=0378-1097&site=1
Citation
Fems Microbiology Letters, 2000, v. 189 n. 2, p. 165-169 How to Cite?
AbstractRNase U2 is an endoribonuclease secreted by the fungus Ustilago sphaerogena. Its genomic DNA (rnu2), containing an intron of 116 bp, has been isolated and cloned. The corresponding cDNA has also been synthesized. The recombinant RNase U2 was successfully produced in Pichia pastoris, fused to the yeast alkaline phosphatase signal peptide. The recombinant RNase U2, purified by affinity chromatography, contains three extra amino acids at its amino-terminal end and retains the enzymatic and spectroscopic properties of the natural fungal protein. (C) 2000 Federation of European Microbiological Societies.
Persistent Identifierhttp://hdl.handle.net/10722/157374
ISSN
2015 Impact Factor: 1.858
2015 SCImago Journal Rankings: 1.126
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorMartínezRuiz, Aen_US
dc.contributor.authorGarcíaOrtega, Len_US
dc.contributor.authorKao, Ren_US
dc.contributor.authorOñaderra, Men_US
dc.contributor.authorMancheño, JMen_US
dc.contributor.authorDavies, Jen_US
dc.contributor.authorMartínez Del Pozo, Aen_US
dc.contributor.authorGavilanes, JGen_US
dc.date.accessioned2012-08-08T08:49:25Z-
dc.date.available2012-08-08T08:49:25Z-
dc.date.issued2000en_US
dc.identifier.citationFems Microbiology Letters, 2000, v. 189 n. 2, p. 165-169en_US
dc.identifier.issn0378-1097en_US
dc.identifier.urihttp://hdl.handle.net/10722/157374-
dc.description.abstractRNase U2 is an endoribonuclease secreted by the fungus Ustilago sphaerogena. Its genomic DNA (rnu2), containing an intron of 116 bp, has been isolated and cloned. The corresponding cDNA has also been synthesized. The recombinant RNase U2 was successfully produced in Pichia pastoris, fused to the yeast alkaline phosphatase signal peptide. The recombinant RNase U2, purified by affinity chromatography, contains three extra amino acids at its amino-terminal end and retains the enzymatic and spectroscopic properties of the natural fungal protein. (C) 2000 Federation of European Microbiological Societies.en_US
dc.languageengen_US
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journal.asp?ref=0378-1097&site=1en_US
dc.relation.ispartofFEMS Microbiology Lettersen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshChromatography, Affinityen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshEndoribonucleases - Genetics - Isolation & Purificationen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshPichia - Geneticsen_US
dc.subject.meshRecombinant Proteins - Genetics - Isolation & Purificationen_US
dc.titleRibonuclease U2: Cloning, production in Pichia pastoris and affinity chromatography purification of the active recombinant proteinen_US
dc.typeArticleen_US
dc.identifier.emailKao, R:rytkao@hkucc.hku.hken_US
dc.identifier.authorityKao, R=rp00481en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/S0378-1097(00)00272-Xen_US
dc.identifier.pmid10930732-
dc.identifier.scopuseid_2-s2.0-0343953000en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0343953000&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume189en_US
dc.identifier.issue2en_US
dc.identifier.spage165en_US
dc.identifier.epage169en_US
dc.identifier.isiWOS:000088681500007-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridMartínezRuiz, A=6701506815en_US
dc.identifier.scopusauthoridGarcíaOrtega, L=6507071173en_US
dc.identifier.scopusauthoridKao, R=7101675499en_US
dc.identifier.scopusauthoridOñaderra, M=7004188455en_US
dc.identifier.scopusauthoridMancheño, JM=6701425928en_US
dc.identifier.scopusauthoridDavies, J=7404982789en_US
dc.identifier.scopusauthoridMartínez Del Pozo, A=35601641400en_US
dc.identifier.scopusauthoridGavilanes, JG=7005888348en_US

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