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. 2010 Apr 21;10(2):M000062-MCP201. doi: 10.1074/mcp.M000062-MCP201

Table II. Summary of peptide data for best transitions studied.

Protein peptide sequence Precursor ion m/z Fragment ion m/z Standard interface
Dual ion funnel interface
LOD CV LOD CV CV at thermo LODa
ng/ml % ng/ml % %
Bovine carbonic anhydrase
    VLDALDSIK 487.28192+ 874.4880+ (y8) 400 20.4 80 23.5 9.7
    DFPIANGER 509.75132+ 378.7036+2 (y72+) 80 38.3 40 36.6 11.6
E. coli β-galactosidase
    VDEDQPFPAVPK 671.33792+ 755.4450+ (y7) 400 45.3 80 24.3 18.2
    LWSAEIPNLYR 681.36422+ 662.3620+ (y5) 4,000b 16.4 4,000b 5.5 5.5
Equine skeletal muscle myoglobin
    LFTGHPETLEK 424.55923+ 506.25892+ (y92+) 80 25.2 80b 5.3 5.3
    YLEFISDAIIHVLHSK 629.01213+ 740.41962+ (y132+) 40,000 9.9 4,000 4.2 10.2
Chicken ovalbumin
    HIATNAVLFFGR 673.37242+ 1,095.5946+ (y10) 40,000b 40.0 40,000b 2.5 2.5
    GGLEPINFQTAADQAR 844.42363+ 666.33882+ (y122+) 4,000 13.0 80 14.9 7.24
Bovine cytochrome c
    EDLIAYLK 482.77112+ 494.2973+ (y4) 400 54.4 80 7.6 3.5
    TGQAPGFSYTDANK 728.83882+ 1,099.5055+ (y10) 400 79.1 40 9.4 11.9

a Percent CV for selected best transitions at the concentration of the LOD for the standard Thermo interface obtained with the dual ion funnel interface.

b Interference peaks from the matrix were observed to limit the detection and quantification of the peaks of interest.