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Aldonate coupling, a simple procedure for the preparation of carbohydrate-protein conjugates for studies of carbohydrate-binding proteins

dc.contributor.authorLonngren, Jorgenen_US
dc.contributor.authorGoldstein, Irwin J.en_US
dc.contributor.authorNiederhuber, John E.en_US
dc.date.accessioned2006-04-07T16:26:58Z
dc.date.available2006-04-07T16:26:58Z
dc.date.issued1976-08en_US
dc.identifier.citationLonngren, Jorgen, Goldstein, Irwin J., Niederhuber, John E. (1976/08)."Aldonate coupling, a simple procedure for the preparation of carbohydrate-protein conjugates for studies of carbohydrate-binding proteins." Archives of Biochemistry and Biophysics 175(2): 661-669. <http://hdl.handle.net/2027.42/21712>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WB5-4DW3KXS-34K/2/72fe7466db7f9fbf7e17e02d405212aden_US
dc.identifier.urihttps://hdl.handle.net/2027.42/21712
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=822335&dopt=citationen_US
dc.description.abstractAldonate coupling a new, high-yield method for conjugation of reducing oligosaccharides to proteins is described. It involves oxidation of the oligosaccharides to their corresponding aldonic acids followed by coupling to amino functions of proteins by activation of carboxyl groups with a water-soluble carbodiimide derivative. The immunochemical properties of some of these synthetic glycoproteins were assessed using several plant agglutinins (lectins) as well as antibodies raised to the conjugates. The scope and limitation of the method are discussed.en_US
dc.format.extent1014702 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleAldonate coupling, a simple procedure for the preparation of carbohydrate-protein conjugates for studies of carbohydrate-binding proteinsen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartments of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, USA: On leave from University of Stockholm, Arrhenius Laboratory, Department of Organic Chemistry, S-10405 Stockholm, Sweden.en_US
dc.contributor.affiliationumDepartments of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, USAen_US
dc.contributor.affiliationumMicrobiology and Surgery, The University of Michigan, Ann Arbor, Michigan 48109, USAen_US
dc.identifier.pmid822335en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/21712/1/0000104.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0003-9861(76)90557-9en_US
dc.identifier.sourceArchives of Biochemistry and Biophysicsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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