Author： Zhu Z. Becklin R.R. desiderio D.M. Dalton J.T.
Publisher： Elsevier
ISSN： 0006-291X
Source： Biochemical and Biophysical Research Communications, Vol.284, Iss.3, 2001-06, pp. : 836-844
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Abstract
An N-terminal hexahistidine-tagged full-length human androgen receptor protein (His6-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 His6-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 His6-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 (Ser308) within the N-terminal transactivation domain of hAR was identified.
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