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Protein-carbohydrate interaction : V. Further inhibition studies directed toward defining the stereochemical requirements of the reactive sites of concanavalin A

dc.contributor.authorSmith, E. E.en_US
dc.contributor.authorGoldstein, Irwin J.en_US
dc.date.accessioned2006-04-17T15:35:26Z
dc.date.available2006-04-17T15:35:26Z
dc.date.issued1967-07en_US
dc.identifier.citationSmithx, E. E., Goldstein, I. J. (1967/07)."Protein-carbohydrate interaction : V. Further inhibition studies directed toward defining the stereochemical requirements of the reactive sites of concanavalin A." Archives of Biochemistry and Biophysics 121(1): 88-95. <http://hdl.handle.net/2027.42/33311>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WB5-4DW39DT-C1/2/2e3a92f74bb62fe9c6c960e7af51dd21en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/33311
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6035073&dopt=citationen_US
dc.description.abstractInhibition studies on the concanavalin A-dextran interaction have been extended using as inhibitors the members of the maltose-, isomaltose-, and methyl [alpha]-isomaltoside series, amino and N-acetyl amino sugars, and a number of oligosaccharides containing more than one linkage type. The interaction of the plant protein at the terminal chain ends of the [alpha]-linked glucans and mannans has been essentially confirmed, and the different characteristic inhibition activities of the linkage types is discussed in terms of steric effects. A possible application of the inhibition technique towards structural analysis of carbohydrate molecules is suggested by the authors.en_US
dc.format.extent687548 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleProtein-carbohydrate interaction : V. Further inhibition studies directed toward defining the stereochemical requirements of the reactive sites of concanavalin Aen_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.affiliationumThe Department of Biochemistry, School of Medicine, State University of New York at Buffalo, Buffalo, New York, U.S.A.; Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan, U.S.A.en_US
dc.contributor.affiliationumThe Department of Biochemistry, School of Medicine, State University of New York at Buffalo, Buffalo, New York, U.S.A.; Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan, U.S.A.en_US
dc.identifier.pmid6035073en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/33311/1/0000706.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0003-9861(67)90012-4en_US
dc.identifier.sourceArchives of Biochemistry and Biophysicsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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