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Analysis of human serum proteins by liquid phase isoelectric focusing and matrix‐assisted laser desorption/ionization‐mass spectrometry
Author(s) -
Wang Michael Z.,
Howard Brandon,
Campa Michael J.,
Patz Edward F.,
Fitzgerald Michael C.
Publication year - 2003
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200300513
Subject(s) - isoelectric focusing , mass spectrometry , chemistry , chromatography , matrix assisted laser desorption/ionization , surface enhanced laser desorption/ionization , isoelectric point , fractionation , protein mass spectrometry , peptide , sample preparation , sample preparation in mass spectrometry , analytical chemistry (journal) , desorption , electrospray ionization , biochemistry , organic chemistry , adsorption , enzyme
Direct matrix‐assisted laser desorption/ionization‐time of flight mass spectrometry (MALDI‐TOF MS) analysis of human serum yielded ion signals from only a fraction of the total number of peptides and proteins expected to be in the sample. We increased the number of peptide and protein ion signals observed in the MALDI‐TOF mass spectra analysis of human serum by using a prefractionation protocol based on liquid phase isoelectric focusing electrophoresis. This pre‐fractionation technique facilitated the MALDI‐TOF MS detection of as many as 262 different peptide and protein ion signals from human serum. The results obtained from three replicate fractionation experiments on the same serum sample indicated that 148 different peptide and protein ion signals were reproducibly detected using our isoelectric focusing and MALDI‐TOF MS protocol.