Carbohydrate binding studies on the lectin from Datura stramonium seeds
dc.contributor.author | Crowley, Jane F. | en_US |
dc.contributor.author | Goldstein, Irwin J. | en_US |
dc.contributor.author | Arnarp, Jan | en_US |
dc.contributor.author | Lonngren, Jorgen | en_US |
dc.date.accessioned | 2006-04-07T18:27:21Z | |
dc.date.available | 2006-04-07T18:27:21Z | |
dc.date.issued | 1984-06 | en_US |
dc.identifier.citation | Crowley, Jane F., Goldstein, Irwin J., Arnarp, Jan, Lonngren, Jorgen (1984/06)."Carbohydrate binding studies on the lectin from Datura stramonium seeds." Archives of Biochemistry and Biophysics 231(2): 524-533. <http://hdl.handle.net/2027.42/24798> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WB5-4DPBW2B-26/2/9deb40fa5e64a6004db60c54c6f30c34 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/24798 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6203486&dopt=citation | en_US |
dc.description.abstract | The carbohydrate-binding properties of the Datura stramonium seed lectin were studied by equilibrium dialysis, quantitative precipitation of natural and synthetic glycoproteins, and hapten inhibition of precipitation. The dimeric lectin (Mr = 86,000) possesses two carbohydrate-binding sites for N,N',N'',N[triple prime]-tetraacetylchitotetritol/mol protein, with an apparent Ka = 8.7 x 103M-1 at 4 [deg]C. Whereas fetuin and orosomucoid reacted poorly with the Datura lectin, the asialo derivatives of these glycoproteins gave strong precipitation with the lectin. Carcinoembryonic antigen, type 14 pneumococcal capsular polysaccharide, and bovine serum albumin, highly substituted with N,N'- diacetylchitobiose units, also precipitated the lectin. Of the homologous series of chitin oligosaccharides tested, N,N',N[triple prime]-triacetylchitotriose was over 6-fold more potent than the disaccharide (N',N'-diacetylchitobiose) which, in turn, was 90 times more reactive than N-acetyl--glucosamine.N-Acetyllactosamine [[beta]--Gal-(1 --> 4)--GlcNAc] was also a potent inhibitor of Datura lectin being equivalent to N,N'-diacetylchitobiose. The requirement for an N-acetyl--glucosaminyl unit linked at the C-4 position was established. The biantennary pentasaccharide (penta-2,6) was a 500-fold more potent inhibitor than N-acetyllactosamine, suggesting that it might interact with both saccharide-binding sites of the Datura lectin simultaneously. | en_US |
dc.format.extent | 909358 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 | Carbohydrate binding studies on the lectin from Datura stramonium seeds | 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 | Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationother | Department of Organic Chemistry, University of Sweden, S-106 91, Stockholm, Sweden | en_US |
dc.contributor.affiliationother | Department of Organic Chemistry, University of Sweden, S-106 91, Stockholm, Sweden | en_US |
dc.identifier.pmid | 6203486 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/24798/1/0000224.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(84)90417-X | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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