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2P-41（2B-O3-M-1735） PDF
Why are the ion yields of hemoglobin α and β different in MALDI MS?
The ion yields of bovine hemoglobin (Hb), which has a tetrameric structure composed of two each of two types of α subunit (Hbα) and β subunit (Hbβ), has been examined by using matrix-assisted laser desorption ionization mass spectrometry (MALDI MS). The ratio of ion yields of analyte ions of Hbα and Hbβ are strongly dependent upon matrix used, although Hbα and Hbβ exist in a ratio of 1:1. In particular, depending on the matrix, the ion yield of Hbβ was remarkably low compared with that of Hbα. Fig.1 shows MALDI mass spectra of Hemoglobin obtained with sinapic acid (SA) and 5-amino-1-naphtol (5,1-ANL) matrix. In this study, the MALDI mass spectra were obtained with several different matrices having benzene and naphthalene skeleton. In addition, we examined the ion yields of the hydrolyzed products of hemoglobin, and relationships between the ion yields and amino acid sequence were discussed.