Isolation and characterization of a second lectin (SNA-II) present in elderberry (Sambucus nigra L.) bark
dc.contributor.author | Kaku, Hanae | en_US |
dc.contributor.author | Peumans, Willy J. | en_US |
dc.contributor.author | Goldstein, Irwin J. | en_US |
dc.date.accessioned | 2006-04-10T13:49:38Z | |
dc.date.available | 2006-04-10T13:49:38Z | |
dc.date.issued | 1990-03 | en_US |
dc.identifier.citation | Kaku, Hanae, Peumans, Willy J., Goldstein, Irwin J. (1990/03)."Isolation and characterization of a second lectin (SNA-II) present in elderberry (Sambucus nigra L.) bark." Archives of Biochemistry and Biophysics 277(2): 255-262. <http://hdl.handle.net/2027.42/28711> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WB5-4DPC1PN-127/2/cc7c4677ca0aae6efe7d1a4f0aa95dab | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/28711 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2310193&dopt=citation | en_US |
dc.description.abstract | A second lectin (SNA-II) has been isolated from elderberry (Sambucus nigra L.) bark by affinity chromatography on immobilized asialo-glycophorin. This lectin is a blood group nonspecific glycoprotein containing 7.8% carbohydrate and which is rich in asparagine/aspartic acid, glutamine/glutamic acid, glycine, valine, and leucine. Gel filtration on Superose 12 gave a single symmetrical peak corresponding to Mr, 51,000; SDS-acrylamide electrophoresis gave a single polypeptide, Mr, 30,000. Hence SNA-II appears to be a homodimer. The lectin is a Gal/GalNAc-specific lectin which is precipitated by glycoproteins containing GalNAc-terminated oligosaccharide chains (e.g., asialo-ovine submaxillary and hog gastric mucins), and by glycoproteins and polysaccharides having multiple terminal nonreducing -galactosyl groups as occur in asialoglycophorin, asialo-laminin and Type 14 pneumococcal polysaccharide. The carbohydrate binding specificity of SNA-II was studied by sugar hapten inhibition of the asialo-glycophorin precipitation reaction. The lectin's binding site appears to be most complementary to GalNAc linked [alpha] to the C-2, C-3, or C-6 hydroxyl group of galactose. These disaccharide units are approximately 100 times more potent than melibiose, 60 times more potent than N-acetyllactosamine, and 30 times more potent than lactose. Interestingly, the blood group A-active trisaccharide containing an -fucosyl group linked [alpha]1-2 to galactose was 10-fold poorer as an inhibitor than the parent oligosaccharide (GalNAc[alpha]1-3Gal), suggesting steric hindrance to binding by the [alpha]--fucosyl group; this explains the failure of the lectin to exhibit blood group A specificity. | en_US |
dc.format.extent | 1072348 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 | Isolation and characterization of a second lectin (SNA-II) present in elderberry (Sambucus nigra L.) bark | 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, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, U.S.A. | en_US |
dc.contributor.affiliationother | Laboratorium voor Plantenbiochemie, Katholieke Universiteit Leuven, Willem de Croylaan 42, B-3030, Leuven (Heverlee, Belgium | en_US |
dc.identifier.pmid | 2310193 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/28711/1/0000532.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(90)90576-K | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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