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Protein-carbohydrate interaction : III. Agar gel-diffusion studies on the interaction of concanavalin A, a lectin isolated from jack bean, with polysaccharides

dc.contributor.authorGoldstein, Irwin J.en_US
dc.contributor.authorSo, Lucy L.en_US
dc.date.accessioned2006-04-13T14:41:36Z
dc.date.available2006-04-13T14:41:36Z
dc.date.issued1965-08en_US
dc.identifier.citationGoldstein, I. J., So, Lucy L. (1965/08)."Protein-carbohydrate interaction : III. Agar gel-diffusion studies on the interaction of concanavalin A, a lectin isolated from jack bean, with polysaccharides." Archives of Biochemistry and Biophysics 111(2): 407-414. <http://hdl.handle.net/2027.42/31996>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WB5-4DW2FW3-11H/2/25084d0219bef8a00d60b54abda9bceden_US
dc.identifier.urihttps://hdl.handle.net/2027.42/31996
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4955563&dopt=citationen_US
dc.description.abstractConcanavalin A, a protein isolated from the jack bean (Canavalia ensiformis), has previously been shown to form a precipitate with glycogen and yeast mannan, and more recently with dextrans and amylopectin. Double-diffusion precipitation studies in agar gel have been found to afford a very sensitive and satisfactory method for investigating the interaction of concanavalin A with certain types of branched, glucose- and mannose- containing polysaccharides. In this manner concanavalin A can be used as a reagent for the detection and preliminary characterization of various types of polysaccharides. Bacterial levans as well as certain plant fructans also form precipitation bands with concanavalin A. This observation represents the first report of such an interaction. The method may also provide an indication as to the heterogeneity of polysaccharide preparations that react with concanavalin A as well as affording preliminary information on the relative molecular size of a series of reactive polysaccharides. Inhibition of the precipitation bands by low molecular weight carbohydrate molecules may be demonstrated. These inhibition studies reveal the highly specific nature of the combining sites of the concanavalin A molecule.en_US
dc.format.extent3460221 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleProtein-carbohydrate interaction : III. Agar gel-diffusion studies on the interaction of concanavalin A, a lectin isolated from jack bean, with polysaccharidesen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USA; Department of Biochemistry, School of Medicine, State University of New York at Buffalo, Buffalo, New York, USA.en_US
dc.contributor.affiliationumDepartment of Biochemistry, School of Medicine, State University of New York at Buffalo, Buffalo, New York, USA; Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USA.en_US
dc.identifier.pmid4955563en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/31996/1/0000038.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0003-9861(65)90203-1en_US
dc.identifier.sourceArchives of Biochemistry and Biophysicsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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