Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1989-7-10
pubmed:abstractText
Rat liver prolactin receptor has been partially characterized and purified to homogeneity using monoclonal antibodies. Pure receptor was digested with trypsin and amino acid sequence of receptor fragments determined. This allowed us to clone the prolactin receptor cDNA. Our approach to clone the receptor cDNA consisted of synthesizing oligonucleotides corresponding to the amino acid sequence of receptor fragments, and to screen a cDNA library. Sequencing reveals that prolactin receptor is a 291 amino acid protein, containing an extracellular domain of 210 residues, a single transmembrane segment of 24 amino acids and a cytoplasmic domain of 57 amino acids. Introduction of the prolactin receptor cDNA into various cell types demonstrates that the single protein is sufficient to bind prolactin with the same affinity and specificity reported for the prolactin receptor.
pubmed:language
fre
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0369-8114
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
215-21
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
[Prolactin receptor: characterization by monoclonal antibodies and cloning of complementary DNA].
pubmed:affiliation
Laboratoire d'Endocrinologie Moléculaire, Université McGill, Hôpital Royal Victoria, Québec, Canada.
pubmed:publicationType
Journal Article, English Abstract