Nanoflow LC/ion mobility/CID/TOF for proteomics: analysis of a human urinary proteome.
A prototype linear octopole ion trap/ion mobility/tandem mass spectrometer has been coupled with a nanoflow liquid chromatography separation approach and used to separate and characterize a complicated peptide mixture from digestion of soluble proteins extracted from human urine. In this approach, two dimensions of separation (nanoflow liquid chromatography and ion mobility) are followed by collision induced dissociation (CID) and mass spectrometry (MS) analysis. From a preliminary analysis of the most intense CID-MS features in a part of the dataset, it is possible to assign 27 peptide ions which correspond to 13 proteins. The data contain many additional CID-MS features for less intense ions. A limited discussion of these features and their potential utility in identifying complicated peptide mixtures required for proteomics study is presented.
Moon
Myeong Hee
MH
Department of Chemistry, Indiana University, Bloomington, Indiana 47405, USA.
Myung
Sunnie
S
Plasencia
Manolo
M
Hilderbrand
Amy E
AE
Clemmer
David E
DE
D000595:Amino Acid Sequence; D002853:Chromatography, Liquid / Q000295:instrumentation / Q000379:methods*; D006801:Humans; D007477:Ions / Q000032:analysis; D013058:Mass Spectrometry / Q000295:instrumentation / Q000379:methods*; D011506:Proteins / Q000032:analysis*; D011507:Proteinuria; D040901:Proteomics; D014556:Urine / Q000737:chemistry*
D007477:Ions; D011506:Proteins