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Immunochemical studies of the combining sites of the two isolectins, A4 and B4, isolated from Bandeiraea simplicifolia

dc.contributor.authorWood, Charlesen_US
dc.contributor.authorKabat, Elvin A.en_US
dc.contributor.authorMurphy, Lee A.en_US
dc.contributor.authorGoldstein, Irwin J.en_US
dc.date.accessioned2006-04-07T17:31:29Z
dc.date.available2006-04-07T17:31:29Z
dc.date.issued1979-11en_US
dc.identifier.citationWood, Charles, Kabat, Elvin A., Murphy, Lee A., Goldstein, Irwin J. (1979/11)."Immunochemical studies of the combining sites of the two isolectins, A4 and B4, isolated from Bandeiraea simplicifolia." Archives of Biochemistry and Biophysics 198(1): 1-11. <http://hdl.handle.net/2027.42/23456>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WB5-4DN47DS-1F0/2/3c8005664dcf6e7840ab56e06d0a5c57en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/23456
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=507832&dopt=citationen_US
dc.description.abstractThe specificity of two isolectins, A4 and B4, of Bandeiraea simplicifolia lectin I (BS-I) was studied by quantitative precipitin, precipitin inhibition, as well as by competitive binding assays using various blood group substances and tritium-labeled human B substance. A4 precipitated well with A1, A2, B, and precursor substances, with A2 precipitating less strongly than did A1 substance; H, Lea and Leb substances did not react. Precipitin inhibition and competitive binding assays confirmed the precipitin data that A4 is most specific for terminal nonreducing [alpha]-linked 2-acetamido-2-deoxy--galactopyranose (GalNAc) but also reacts with oligosaccharides with terminal nonreducing [alpha]-linked Gal, thus accounting for its blood group A and B specificities. Of the oligosaccharides tested, A4 reacted best with GalNAc[alpha]1 --&gt; 3Gal and a trisaccharide GalNAc[alpha]1 --&gt; 3Gal[beta]1 --&gt; 3GlcNAc (A5II) was equally active, suggesting that the A4 site is no larger than a disaccharide. B4 precipitated well with B substances and with a precursor substance to a lesser extent, while A1 A2, H, Lea, and Leb substances were inactive. Precipitin and competitive binding assays showed that it reacted well with oligosaccharides with terminal [alpha]-linked Gal with Gal[alpha]1 --&gt; 3Gal being most active, while Fuc[alpha]l --&gt; 2 Gal[alpha]1 --&gt; 3Gal[beta]1 --&gt; 4GlcNAc[beta]1 --&gt; 6-R (BRL 0.44) was much less active, indicating a substitution at the subterminal residue affects the binding substantially and indicating that the B4 site involves at least the subterminal [alpha]1 --&gt; 3 linked Gal. The B4 site was found to be strictly B specific.en_US
dc.format.extent856190 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
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dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleImmunochemical studies of the combining sites of the two isolectins, A4 and B4, isolated from Bandeiraea simplicifoliaen_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.affiliationumDepartments of Microbiology, Human Genetics and Development, and Neurology, and the Cancer Center, Columbia University College of Physicians and Surgeons, New York, New York 10032, USA; Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USAen_US
dc.contributor.affiliationumDepartments of Microbiology, Human Genetics and Development, and Neurology, and the Cancer Center, Columbia University College of Physicians and Surgeons, New York, New York 10032, USA; Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USAen_US
dc.contributor.affiliationumDepartments of Microbiology, Human Genetics and Development, and Neurology, and the Cancer Center, Columbia University College of Physicians and Surgeons, New York, New York 10032, USA; Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USAen_US
dc.contributor.affiliationumDepartments of Microbiology, Human Genetics and Development, and Neurology, and the Cancer Center, Columbia University College of Physicians and Surgeons, New York, New York 10032, USA; Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USAen_US
dc.identifier.pmid507832en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/23456/1/0000407.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0003-9861(79)90389-8en_US
dc.identifier.sourceArchives of Biochemistry and Biophysicsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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