Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1986-4-3
pubmed:abstractText
We have used a new methodology to generate a monospecific antiserum to the corticotropin (ACTH) receptor on mouse Y-1 adrenal cells. Using immunoaffinity chromatography the ACTH receptor was purified, and the molecular structure and 125I-ACTH binding characteristics were determined. A molecular weight (Mr) of 225 000 was determined for the complete ACTH receptor as analyzed by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The receptor was composed of 4 subunits with Mr 83 000, 64 000, 52 000 and 22 000. The 83 and 52 kDa subunits were disulfide linked and non-covalently associated with the 64 and 22 kDa subunits. The ability to specifically bind 125I-ACTH was localized to the 83 kDa subunit. The purified receptor possessed binding affinities of 3.4 X 10(10) M-1 and 1.0 X 10(9) M-1 as determined by Scatchard analysis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0303-7207
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Molecular characterization of a corticotropin (ACTH) receptor.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't