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Purification and characterization of a new mannose-specific lectin from Sternbergia lutea bulbs
dc.contributor.authorSaito, Keikoen_US
dc.contributor.authorMisaki, Akiraen_US
dc.contributor.authorGoldstein, Irwin J.en_US
dc.date.accessioned2006-09-11T16:24:21Z
dc.date.available2006-09-11T16:24:21Z
dc.date.issued1997-01en_US
dc.identifier.citationSaito, Keiko; Misaki, Akira; Goldstein, Irwin J.; (1997). "Purification and characterization of a new mannose-specific lectin from Sternbergia lutea bulbs." Glycoconjugate Journal 14(8): 889-896. <http://hdl.handle.net/2027.42/45734>en_US
dc.identifier.issn0282-0080en_US
dc.identifier.issn1573-4986en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/45734
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=9486421&dopt=citationen_US
dc.description.abstractA new mannose-binding lectin was isolated from Sternbergia lutea bulbs by affinity chromatography on an α(1-2)mannobiose-Synsorb column and purified further by gel filtration. This lectin (S. lutea agglutinin; SLA) appeared homogeneous by native-gel electrophoresis at pH 4.3, gel filtration chromatography on a Sephadex G-75 column, and SDS-polyacrylamide gel electrophoresis, These data indicate that SLA is a dimeric protein (20 kDa) composed of two identical subunits of 10 kDa which are linked by non-covalent interactions.en_US
dc.format.extent659095 bytes
dc.format.extent3115 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherKluwer Academic Publishers; Chapman and Hall ; Springer Science+Business Mediaen_US
dc.subject.otherLife Sciencesen_US
dc.subject.otherPathologyen_US
dc.subject.otherBiochemistry, Generalen_US
dc.subject.otherSternbergia Luteaen_US
dc.subject.otherMannose-binding Lectinen_US
dc.titlePurification and characterization of a new mannose-specific lectin from Sternbergia lutea bulbsen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbsecondlevelDentistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, 48109, USAen_US
dc.contributor.affiliationotherFaculty of Human Life Science, Osaka City University, Osaka, 558, Japanen_US
dc.contributor.affiliationotherFaculty of Human Life Science, Osaka City University, Osaka, 558, Japanen_US
dc.contributor.affiliationumcampusAnn Arboren_US
dc.identifier.pmid9486421en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/45734/1/10719_2004_Article_173163.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1023/A:1018558509466en_US
dc.identifier.sourceGlycoconjugate Journalen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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