posted on 2015-08-18, 00:00authored bySameh Magdeldin, Amr Elguoshy, Yutaka Yoshida, Yoshitoshi Hirao, Bo Xu, Ying Zhang, Keiko Yamamoto, Hiroki Takimoto, Hidehiko Fujinaka, Naohiko Kinoshita, Tadashi Yamamoto
OFFGEL
fractionation of mouse kidney protein lysate and its tryptic
peptide digest has been examined in this study for better understanding
the differences between protein and peptide fractionation methods
and attaining maximum recruitment of this modern methodology for in-depth
proteomic analysis. With the same initial protein/peptide load for
both fractionation methods, protein OFFGEL fractionation showed a
preponderance in terms of protein identification, fractionation efficiency,
and focusing resolution, while peptide OFFGEL was better in recovery,
number of peptide matches, and protein coverage. This result suggests
that the protein fractionation method is more suitable for shotgun
analysis while peptide fractionation suits well quantitative peptide
analysis [isobaric tags for relative and absolute quantitation (iTRAQ)
or tandem mass tags (TMT)]. Taken together, utilization of the advantages
of both fractionation approaches could be attained by coupling both
methods to be applied on complex biological tissue. A typical result
is shown in this article by identification of 8262 confident proteins
of whole mouse kidney under stringent condition. We therefore consider
OFFGEL fractionation as an effective and efficient addition to both
label-free and quantitative label proteomics workflow.