Equilibrium dialysis and carborydrate-binding studies on the 2-acetamido-2-deoxy--glucopyranosyl-binding lectin from bandeiraea simplicifolia seeds
dc.contributor.author | Ebisu, Shigeyuki | en_US |
dc.contributor.author | Iyer, P. N. Shankar | en_US |
dc.contributor.author | Goldstein, Irwin J. | en_US |
dc.date.accessioned | 2006-04-07T17:02:30Z | |
dc.date.available | 2006-04-07T17:02:30Z | |
dc.date.issued | 1978-03 | en_US |
dc.identifier.citation | Ebisu, Shigeyuki, Iyer, P. N. Shankar, Goldstein, Irwin J. (1978/03)."Equilibrium dialysis and carborydrate-binding studies on the 2-acetamido-2-deoxy--glucopyranosyl-binding lectin from bandeiraea simplicifolia seeds." Carbohydrate Research 61(1): 129-138. <http://hdl.handle.net/2027.42/22639> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6TFF-42HG8VW-4K/2/4ec1f222b878ed9ceb8b4eb6fd67c18b | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/22639 | |
dc.description.abstract | The carbohydrate-binding specificity of Bandeiraea simplicifolia lectin II (BS II lectin) has been studied by quantitative precipitin and hapten-inhibition analysis. The BS II lectin precipitated biopolymers having nonreducing 2-acetamido-2-deoxy--glucopyranosyl residues, such as antigen A. Dextran B-1355-S and rabbit-liver glycogen also afforded precipitin curves with high concentrations of the BS II lectin. Phenyl 2-acetamido-2-deoxy-[alpha]--glucopyranoside and p-nitrophenyl 2-acetamido-2-deoxy-[alpha]--glucopyranoside, the best inhibitors of the BS II lectin-p-azophenyl 2-acetamido-2-deoxy-[beta]--glucopyranoside-bovine serum albumin conjugate precipitin-system, were 4 times as active as 2-acetamido-2-deoxy--glucopyranose. Of the free monosaccharides tested, 2-acetamido-2-deoxy--glucopyranose was the most potent inhibitor, being over 100 times better than -fructose and 400 times better than -glucose. Comparison of the inhibiting capacity of methyl or p-nitrophenyl 2-acetamido-2-deoxy-[alpha]--glucopyranoside with their corresponding [beta] anomers showed that the [alpha] anomer was bound 6 to 8 times more avidly than the [beta] anomer. Replacement of the C-3, C-4, or C-6 hydroxyl group of -glucose by a methoxyl group or a fluorine atom abolished the capacity of the resulting sugar to bind the BS II lectin, but substitution of the C-2 hydroxyl group of -glucose, by either a methoxyl group or a fluorine group, had no appreciable effect on binding to the lectin. N,N'-Diacetylchitobiose was as active as N,N',N"-triacetylchitotriose, and they were both twice as potent as disaccharides having a nonreducing 2-acetamido-2-deoxy-[beta]--glucopyranosyl residue. Disaccharides having [beta]--(1 --> 6) glycosidic bonds were very poor inhibitors. Equilibrium-dialysis experiments with p-nitrophenyl 2-acetamido-2-deoxy-[alpha]--glucopyranoside as binding ligand indicated that the BS II lectin possesses approximately one carbohydrate-binding siteper subunit for the tetrameric protein (Mr 113,000), with association constants of 1.3 x 105 M-1 at 4[deg], and 0.4 x 105 M-1 at 37[deg]. | en_US |
dc.format.extent | 764364 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 | Equilibrium dialysis and carborydrate-binding studies on the 2-acetamido-2-deoxy--glucopyranosyl-binding lectin from bandeiraea simplicifolia seeds | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | 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 | Deparment of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109 U.S.A. | en_US |
dc.contributor.affiliationum | Deparment of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109 U.S.A. | en_US |
dc.contributor.affiliationum | Deparment of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109 U.S.A. | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/22639/1/0000190.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/S0008-6215(00)84473-0 | en_US |
dc.identifier.source | Carbohydrate Research | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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