Elderberry bark lectin-gold techniques for the detection of Neu5Ac (α2,6) Gal/GalNAc sequences: applications and limitations
dc.contributor.author | Taatjes, D. J. | en_US |
dc.contributor.author | Roth, Jürgen | en_US |
dc.contributor.author | Peumans, Willy J. | en_US |
dc.contributor.author | Goldstein, Irwin J. | en_US |
dc.date.accessioned | 2006-09-08T20:47:48Z | |
dc.date.available | 2006-09-08T20:47:48Z | |
dc.date.issued | 1988-09 | en_US |
dc.identifier.citation | Taatjes, D. J.; Roth, J.; Peumans, W.; Goldstein, I. J.; (1988). "Elderberry bark lectin-gold techniques for the detection of Neu5Ac (α2,6) Gal/GalNAc sequences: applications and limitations." The Histochemical Journal 20(9): 478-490. <http://hdl.handle.net/2027.42/42854> | en_US |
dc.identifier.issn | 0018-2214 | en_US |
dc.identifier.issn | 1573-6865 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/42854 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2467894&dopt=citation | en_US |
dc.description.abstract | The lectin from the elderberry ( Sambucus nigra L.) bark, shown to recognize the sequence neuraminic acid (α2,6) galactose/ N -acetylgalactosamine, was applied for detecting binding sites in Lowicryl K4M sections by light and electron microscopy. The lectin was used either directly complexed to colloidal gold or in a two-step cytochemical affinity technique. The lectin-gold complex proved to be superior and thus was extensively tested on rat liver, kidney and hepatoma cells as well as on sheep and bovine submandibular glands. Controls to establish specificity of lectin-gold binding included sugar and glycoprotein inhibition tests and enzymic removal of sialic acid. In agreement with biochemical data demonstrating the potentiating effect of sialic acid on the binding of the lectin to oligosaccharides, enzymic removal of sialic acid from liver sections resulted in abolition of lectin staining. However, in the submandibular glands, neuraminidase pretreatment of the sections had no effect on the subsequent lectin-gold binding. In rat kidney some structures became negative while others retained the lectin-gold staining due to binding to penultimate. N -acetylgalactosamine exposed after sialic acid removal. In line with this, spot blot analysis demonstrated that the lectin-gold complex reacted with both fetuin and asialofetuin. Taken together, these results suggest that, for cytochemical staining, the sialic acid and the galactose/ N -acetylgalactosamine lectin combining subsites of Sambucus nigra L. lectin are equally reactive with cellular glycoconjugates and that neuraminidase predigestion of tissue sections is of utmost importance to ensure specificity of staining for the sequence neuraminic acid (α2,6) galactose/ N -acetylgalactosamine. | en_US |
dc.format.extent | 5709291 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers; Chapman and Hall Ltd. ; Springer Science+Business Media | en_US |
dc.subject.other | Life Sciences | en_US |
dc.subject.other | Biomedicine General | en_US |
dc.subject.other | Cell Biology | en_US |
dc.subject.other | Animal Anatomy / Morphology / Histology | en_US |
dc.subject.other | Biological Microscopy | en_US |
dc.title | Elderberry bark lectin-gold techniques for the detection of Neu5Ac (α2,6) Gal/GalNAc sequences: applications and limitations | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | 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, 48109, Ann Arbor, Michigan, USA | en_US |
dc.contributor.affiliationother | Interdepartmental Electron Microscopy, Biocenter, University of Basle, Klingelbergstr. 70, CH-4056, Basle, Switzerland | en_US |
dc.contributor.affiliationother | Interdepartmental Electron Microscopy, Biocenter, University of Basle, Klingelbergstr. 70, CH-4056, Basle, Switzerland | en_US |
dc.contributor.affiliationother | Laboratorium voor Plantenbiochemie, Katholeik Universiteit Leuven, B-3030, Leuven (Heverlee), Belgium | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 2467894 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/42854/1/10735_2005_Article_BF01002646.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/BF01002646 | en_US |
dc.identifier.source | The Histochemical Journal | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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