Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1975-5-10
pubmed:abstractText
The nature of the receptor sites for several agglutinins is characterized by hemagglutination inhibition assays. The inhibitory activity of human erythrocytes glycoproteins, from which sialic acid, sialic acid and galactose or alkali-labile oligosaccharides have been removed, is compared to the inhibitory effect of compounds with known structure. It is shown that the lectin from Arachis hypogea and anti-T bind to alkali-labile galactosyl-residues. Agglutinins from Bauhinia purpurea and variegata (non- or N-specific), Maclura aurantiaca, Iberis amara, sempervirens, umbellata hybrida and umbellata nana (M- or nonspecific), Moluccella laevis (A- plus N-specific), Helix pomatia, Helix aspersa, Helix lucorum and Caucasotachea atrolabiata interact with alkali-labile N-acetylgalactosamine. The results obtained with the anti-A agglutinins from various snails suggest that human erythrocyte glycoproteins contain, besides the alkali-labile tetrasaccharide, a peptide-linked sialyl-N-acetyl-galactosaminyl-residue. The investigations do not allow a precise definition of the receptor sites for the lectins having M- or N-specificity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0042-9007
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
133-48
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Further characterization of some heterophile agglutinins reacting with alkali-labile carbohydrate chains of human erythrocyte glycoproteins.
pubmed:publicationType
Journal Article, Comparative Study