Immunochemical studies of the combining sites of the two isolectins, A4 and B4, isolated from Bandeiraea simplicifolia
dc.contributor.author | Wood, Charles | en_US |
dc.contributor.author | Kabat, Elvin A. | en_US |
dc.contributor.author | Murphy, Lee A. | en_US |
dc.contributor.author | Goldstein, Irwin J. | en_US |
dc.date.accessioned | 2006-04-07T17:31:29Z | |
dc.date.available | 2006-04-07T17:31:29Z | |
dc.date.issued | 1979-11 | en_US |
dc.identifier.citation | Wood, 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.uri | http://www.sciencedirect.com/science/article/B6WB5-4DN47DS-1F0/2/3c8005664dcf6e7840ab56e06d0a5c57 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/23456 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=507832&dopt=citation | en_US |
dc.description.abstract | The 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 --> 3Gal and a trisaccharide GalNAc[alpha]1 --> 3Gal[beta]1 --> 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 --> 3Gal being most active, while Fuc[alpha]l --> 2 Gal[alpha]1 --> 3Gal[beta]1 --> 4GlcNAc[beta]1 --> 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 --> 3 linked Gal. The B4 site was found to be strictly B specific. | en_US |
dc.format.extent | 856190 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Immunochemical studies of the combining sites of the two isolectins, A4 and B4, isolated from Bandeiraea simplicifolia | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Departments 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, USA | en_US |
dc.contributor.affiliationum | Departments 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, USA | en_US |
dc.contributor.affiliationum | Departments 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, USA | en_US |
dc.contributor.affiliationum | Departments 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, USA | en_US |
dc.identifier.pmid | 507832 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/23456/1/0000407.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(79)90389-8 | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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