Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-6-8
pubmed:abstractText
An N-terminal hexahistidine-tagged full-length human androgen receptor protein (His(6)-hAR) was overexpressed and purified to apparent homogeneity in the presence of dihydrotestosterone (DHT) in our previous studies. In-gel trypsin digestion of the purified DHT-bound His(6)-hAR, and tryptic peptide mapping using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI/TOF-MS), detected a total of 17 peptides (21% coverage of hAR) with 9 peptides originating from the ligand-binding domain (LBD, 31% coverage of LBD). Amino acid sequencing analysis of the tryptic peptides from a separate in-gel digestion of the His(6)-hAR, using HPLC-coupled electrospray ionization ion trap mass spectrometry (LC/ESI-ITMS and MS/MS), unambiguously confirmed 21 peptides with 19% coverage of the hAR, of which 11 peptides originated from the LBD (35% coverage of LBD). These 21 peptides included 11 out of the 17 peptides detected by MALDI/TOF-MS. In addition, a novel serine phosphorylation site (Ser(308)) within the N-terminal transactivation domain of hAR was identified.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
284
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
836-44
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11396978-Amino Acid Sequence, pubmed-meshheading:11396978-Cells, Cultured, pubmed-meshheading:11396978-Chromatography, High Pressure Liquid, pubmed-meshheading:11396978-Histidine, pubmed-meshheading:11396978-Humans, pubmed-meshheading:11396978-Molecular Sequence Data, pubmed-meshheading:11396978-Peptide Mapping, pubmed-meshheading:11396978-Peptides, pubmed-meshheading:11396978-Phosphorylation, pubmed-meshheading:11396978-Phosphoserine, pubmed-meshheading:11396978-Protein Structure, Tertiary, pubmed-meshheading:11396978-Receptors, Androgen, pubmed-meshheading:11396978-Recombinant Fusion Proteins, pubmed-meshheading:11396978-Spectrometry, Mass, Electrospray Ionization, pubmed-meshheading:11396978-Spectrometry, Mass, Matrix-Assisted Laser..., pubmed-meshheading:11396978-Trypsin
pubmed:year
2001
pubmed:articleTitle
Identification of a novel phosphorylation site in human androgen receptor by mass spectrometry.
pubmed:affiliation
Division of Pharmaceutics and Pharmaceutical Chemistry, College of Pharmacy, Ohio State University, Columbus, Ohio 43210, USA.
pubmed:publicationType
Journal Article, 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