Linked Life Data

1382578

Source:http://linkedlifedata.com/resource/pubmed/id/1382578

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
1992-10-26
pubmed:abstractText
We have previously shown that plant lectins with a wide range of carbohydrate binding specificities can bind and cross-link (precipitate) specific multiantennary oligosaccharides and glycopeptides [cf. Bhattacharyya, L., Fant, J., Lonn, H., & Brewer, C. F. (1990) Biochemistry 29, 7523-7530]. This leads to a new source of binding specificity: namely, the formation of homogeneous cross-linked lattices between lectins and carbohydrates. Recently, we have demonstrated the existence of highly ordered cross-linked lattices that form between the D-Man/D-Glc-specific plant lectin concanavalin A and the soybean agglutinin which is a tetrameric glycoprotein possessing a single Man9 oligomannose chain per monomer [Khan, M. I., Mandal, D. K., & Brewer, C. F. (1991) Carbohydr. Res. 213, 69-77]. In the present study, we have compared the ability of the 14-kDa beta-galactoside-specific lectin from calf spleen, a dimeric S-type animal lectin, and several galactose-specific plant lectins from Erythrina indica, Erythrina cristagalli, and Glycine max (soybean agglutinin) to form specific cross-linked complexes with asialofetuin (ASF), a 48-kDa monomeric glycoprotein, using quantitative precipitation analyses. The results show the formation of 1:9 and 1:3 stoichiometric cross-linked complexes (per monomer) of ASF to the 14-kDa lectin, depending on their relative ratio in solution. Evidence indicates that the three triantennary N-linked complex-type oligosaccharide chains of ASF mediate the cross-linking interactions and that each chain expresses either trivalency in the 1:9 cross-linked complex or univalency in the 1:3 complex.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8465-72
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:1382578-Animals, pubmed-meshheading:1382578-Asialoglycoproteins, pubmed-meshheading:1382578-Carbohydrate Conformation, pubmed-meshheading:1382578-Carbohydrate Sequence, pubmed-meshheading:1382578-Cattle, pubmed-meshheading:1382578-Chemical Precipitation, pubmed-meshheading:1382578-Cross-Linking Reagents, pubmed-meshheading:1382578-Fetuins, pubmed-meshheading:1382578-Galactosides, pubmed-meshheading:1382578-Lectins, pubmed-meshheading:1382578-Macromolecular Substances, pubmed-meshheading:1382578-Models, Structural, pubmed-meshheading:1382578-Molecular Sequence Data, pubmed-meshheading:1382578-Oligosaccharides, pubmed-meshheading:1382578-Plant Lectins, pubmed-meshheading:1382578-Plants, pubmed-meshheading:1382578-Spleen, pubmed-meshheading:1382578-Substrate Specificity, pubmed-meshheading:1382578-alpha-Fetoproteins
pubmed:year
1992
pubmed:articleTitle
Cross-linking activity of the 14-kilodalton beta-galactoside-specific vertebrate lectin with asialofetuin: comparison with several galactose-specific plant lectins.
pubmed:affiliation
Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.