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Figure 4 | Proteome Science

Figure 4

From: Proteomic analysis of plasma membranes isolated from undifferentiated and differentiated HepaRG cells

Figure 4

MS/MS spectra of precursor ions that correspond to peptides that are part of Annexin A2, Annexin A1, S100A10, or Annexin A5. (A) A triple-charged peak at m/z of 551.27 (expanded in the inbox) was fragmented by MS/MS and produced a MS/MS spectrum. Fragmentation of the peptide backbone in the MS/MS produced a series of b and y peaks, marked in the MS/MS. Data analysis of the b and y peaks from the MS/MS spectrum led to identification of a peptide with the sequence SALSGHLETVILGLLK, which was part of Annexin A2 protein. (B): A double-charged peak at m/z of 803.53 (expanded in the inbox) was fragmented by MS/MS and produced a MS/MS spectrum. Data analysis of the MS/MS spectrum led to identification of a peptide with the sequence ALTGHLEEVVLALLK, which was part of Annexin A1 protein. (C) A double-charged peak at m/z of 550.57 (expanded in the inbox) was fragmented by MS/MS and produced a MS/MS spectrum. Data analysis of this MS/MS spectrum led to identification of a peptide with the sequence FAGDKGYLTK, which was part of S100A10 protein. (D) A double-charged peak at m/z of 618.07 (expanded in the inbox) was fragmented by MS/MS and produced a MS/MS spectrum. Data analysis of this MS/MS spectrum led to identification of a peptide with the sequence SEIDLFNIRK, which was part of Annexin A5 protein.

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