Matrix-assisted laser desorption ionization time of flight tandem mass spectrometry and electrospray ionization quadrupole time of flight mass spectrometry protein.doc

 PAGE \* MERGEFORMAT 18 Matrix-assisted laser desorption ionization time of flight tandem mass spectrometry and electrospray ionization quadrupole time of flight mass spectrometry protein Of: Ni Ma Guoxin Zhu Lei Wei Liu Jianhua Hu Xiaofang Xu Xuemin soil [Abstract] Comparison of matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI TOF TOF) and electrospray ionization quadrupole time of flight mass spectrometry (ESI Q TOF) in the protein analysis of qualitative and quantitative performance, respectively, using two The instrument used for relative and absolute quantification of the same amount of ectopic labeling (iTRAQ) markers of estrogen stimulation of MCF7 cells before and after hydrolysis of protein peptide were qualitative and quantitative analysis. results show that MALDI TOF TOF and ESI Q TOF 1086 kinds of methods were identified and 848 kinds of proteins, including 633 kinds of the same protein; MALDI TOF TOF and ESI Q TOF methods were 38 and 33 found differences in the expression of more than 0.5 times the protein, which is the same protein 3 . experimental data shows that the two instruments in the qualitative and quantitative analysis of proteins is very complementary to the two instruments in combination, can significantly improve not only the qualitative and quantitative analysis of protein coverage and analysis can increase confidence. [Keywords:] equal ectopic label, matrix-assisted laser desorption ionization time of flight mass spectrometry, electrospray ionization quadrupole time of flight mass spectrometry, qualitative analysis, quantitative analysis 1 Introduction Matrix-assisted laser desorption ionization (MALDI) and electrospray ionization (ESI) is currently used for peptide and protein ionization in two main ways. This peptide ion of the two methods has a highly complementary [1]. The results show that, MALDI basic amino acid residues favor the ionization [2], ESI is conducive to hydrophobic