Linked Life Data

6838883

Source:http://linkedlifedata.com/resource/pubmed/id/6838883

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1983-6-23
pubmed:abstractText
Glycophorin was prepared from dog erythrocyte membranes by extraction with lithium diiodosalicylate and partition in aqueous phenol. Tryptic and chymotryptic treatments of the glycophorin produced two major glycopeptides labeled T1 and CH1, respectively. The glycopeptides were isolated by gel chromatography followed by ion-exchange chromatography, and subjected to amino acid sequence analysis. Both glycopeptides represented the amino-terminal domain of the major dog glycophorin; T1 of 52 residues and CH1 of 43 residues. The amino-terminal sequence of dog glycophorin does not have significant homology with those of human, horse or porcine glycophorins. This result is in good agreement with our previous proposal that there is no homology in the sequence of the amino-terminal glycosylated domain of glycophorin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
742
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
477-83
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Amino acid sequence and oligosaccharide attachment sites of the glycosylated domain of dog erythrocyte glycophorin.
pubmed:publicationType
Journal Article