Linked Life Data

7518456

Source:http://linkedlifedata.com/resource/pubmed/id/7518456

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1994-8-18
pubmed:abstractText
When young and senescent erythrocytes, separated from freshly collected human blood, were incubated with 125I-goat anti-human IgG, binding of the IgG to the senescent cells was three times as high as that to the young cells. The release of the radioactivity from the anti-human IgG-bound senescent cells was enhanced by incubation with band 3 oligosaccharides but not by those digested with endo-beta-galactosidase or neuraminidase. The senescent cells whose surface band 3 saccharide chains were cleaved by endo-beta-galactosidase or totally removed by N-glycosidase F showed decreased binding of the anti-human IgG. The radioactivity was effectively released from the anti-human IgG-bound senescent cells by digestion with endo-beta-galactosidase. The results suggest that senescent erythrocytes bind anti-band 3 autoantibody, and the antigenic sites on the cell surface are sialylated poly-N-acetyllactosaminyl sugar chains of band 3 glycoprotein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19394-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Involvement of sialylated poly-N-acetyllactosaminyl sugar chains of band 3 glycoprotein on senescent erythrocytes in anti-band 3 autoantibody binding.
pubmed:affiliation
Tokyo College of Pharmacy, Japan.
pubmed:publicationType
Journal Article, Comparative Study