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Figure 1 | BMC Biochemistry

Figure 1

From: Possibilities and pitfalls in quantifying the extent of cysteine sulfenic acid modification of specific proteins within complex biofluids

Figure 1

Mass spectra of A) albumin and B) TTR extracted from human plasma that was treated with/without hydrogen peroxide and with/without the dimedone-based Cys-SOH trapping reagent CPPCHD. For albumin (A), deconvoluted "MH+" peaks are assigned as follows: 66438 = Native/unmodified (Calc. 66439), 66557 = S-Cysteinylated (Calc. 66558), 66600 = Glycated native form (Calc. 66601), 66614 = S-CysGly (Calc. 66615), 66719 = Glycated S-Cysteinylated form (Calc. 66720), 66818 = CPPCHD-modified native form (Calc. 66819). For TTR (B), 13761 = Native/unmodified (Calc. 13762), 13793 = Cys-sulfinic acid (SO2H) due to over oxidation (Calc. 13794), 13880 = S-Cysteinylated (Calc. 13881), 13937 = S-CysGly (Calc. 13938), 14067 = S-Glutathionylated (Calc. 14069), 14141 = CPPCHD-modified native form (Calc. 14142). For TTR, partial peak splitting is due to incomplete monoisotopic resolution. Assigned "MH+" values in deconvoluted spectra are centroided average masses.

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BMC Biochemistry

ISSN: 1471-2091

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