Linked Life Data

2701177

Source:http://linkedlifedata.com/resource/pubmed/id/2701177

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1990-9-4
pubmed:abstractText
Partial proteolytic digestion of the mammary prolactin (PRL) receptor was used to generate receptor fragments and analyze their immunoreactivity and PRL binding properties. Tryptic digestion of the PRL receptor produced two immunoreactive fragments (Mr approximately 30,000 and approximately 15,000) that reacted with a monoclonal anti-PRL receptor antibody and still specifically bound PRL, while the complete immunoreactive PRL binding unit (Mr approximately 42,000) disappeared. Neither chymotrypsin nor V8 protease were able to generate any immunoreactive receptor fragments. These receptor fragments may represent smaller PRL binding receptor form(s) of biological significance.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0197-5110
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
479-93
pubmed:dateRevised
2006-7-19
pubmed:meshHeading
pubmed:articleTitle
Partial proteolytic digestion of the mammary prolactin receptor: identification of smaller prolactin binding fragments.
pubmed:affiliation
Unité d'Endocrinologie Moléculaire, Institut National de la Recherche Agronomique, Jouy-en-Josas, France.
pubmed:publicationType
Journal Article