Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5-6
pubmed:dateCreated
1985-10-7
pubmed:abstractText
The human Thy-1 homologue (p25) was characterized biochemically for amino acid composition, sequence and carbohydrate content. Two other forms of the human Thy-1 molecule were detected and partially characterized. A 40,000 mol.wt. molecule (p40) is the dimer of p25 and its formation is increased by the presence of sodium dodecyl sulphate (SDS). The second form of 16,000 mol.wt. (p16) appears to be a cryptic or breakdown form of p25. Comparison of the amino acid compositions of p25, p40 and p16 isolated from MOLT-3 cells, with that deduced from the nucleotide sequence of the gene coding for part of the putative T cell antigen receptor, also from MOLT-3 cells, shows that the Thy-1 homologue is distinct from, but evolutionary related to, one of the putative T cell antigen receptor polypeptide chains.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0305-1811
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
283-96
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:articleTitle
Biochemical characterization of human Thy-1.
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., Research Support, Non-U.S. Gov't