Application of slicing of one-dimensional gels with subsequent slice-by-slice mass spectrometry for the proteomic profiling of human liver cytochromes P450.
Sequential thin slicing of one-dimensional electrophoresis gels followed by slice-by-slice mass spectrometry to allow protein identification was used to produce a proteomic map for cytochromes P450. Parallel MALDI-TOF-MS and LC-MS/MS analyses were performed. Combination of the two MS methods increased the quality of protein identification. We have proposed an efficient approach to obtain a comprehensive profile of drug-metabolizing enzymes in the liver that can be used to differentiate between polymorphic variants of cytochromes P450.
Lisitsa
Andrey V
AV
Institute of Biomedical Chemistry, Russian Academy of Medical Sciences, Moscow, Russia.
Petushkova
Natalia A
NA
Thiele
Herbert
H
Moshkovskii
Sergei A
SA
Zgoda
Viktor G
VG
Karuzina
Irina I
II
Chernobrovkin
Aleksey L
AL
Skipenko
Oleg G
OG
Archakov
Alexander I
AI
D000595:Amino Acid Sequence; D003577:Cytochrome P-450 Enzyme System / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D006801:Humans; D008099:Liver / Q000201:enzymology*; D013058:Mass Spectrometry / Q000379:methods*; D008862:Microsomes, Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D010455:Peptides / Q000032:analysis / Q000235:genetics; D040901:Proteomics / Q000379:methods*
D010455:Peptides; D003577:Cytochrome P-450 Enzyme System