原创力文档Gel based mass spectrometric analysis of a strongly hydrophobic GABAA receptor subunit containing four transmembrane domains英文文献.pdfVIP
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PROTOCOL
Gel-based mass spectrometric analysis of a strongly
hydrophobic GABAA-receptor subunit containing four
transmembrane domains
1 2 2 1 3 1
Sung-Ung Kang , Karoline Fuchs , Werner Sieghart , Arnold Pollak , Edina Csaszar Gert Lubec
1Department of Pediatrics, Medical University of Vienna, Vienna, Austria. 2Division of Biochemistry and Molecular Biology, Center for Brain Research, Medical
University of Vienna, Vienna, Austria. 3Mass Spectrometry Facility, Max F. Perutz Laboratories, Vienna, Austria. Correspondence should be addressed to G.L.
(gert.lubec@meduniwien.ac.at).
s
l Published online 2 July 2009; doi:10.1038/nprot.2009.92
o
c
o
t
o The analysis of highly hydrophobic proteins is still an analytical challenge. Using a recombinant gamma-aminobutyric acid A
r
p
e (GABA )-receptor subunit as a model protein, we developed a gel-based proteomic approach for high MS/MS-peptide sequence coverage
A
r
u
t identification. Protein samples were separated by multi-dimensional gel electrophoresis and the three protein spots representing the
a
n
/ GABAA-receptor subunit a-1 from the last electrophoretic step were used for in-gel digestion with trypsin, chymotrypsin and subtilisin,
m
o followed by subsequent mass-spectrometric identification by nano-ESI-LC-MS/MS Qstar XL (quadrupole time-of-flight (qQTOF)) and
c
.
e linear ion trap (LIT) LTQ XL identification. This protocol allows the unambiguous identification of the GABAA-receptor a-1 subunit
r
u
t protein with 100% sequence coverage, thus covering all four hydrophobic transmembrane
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