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. Author manuscript; available in PMC: 2016 Dec 1.
Published in final edited form as: Toxicol Appl Pharmacol. 2015 Oct 3;289(2):155–162. doi: 10.1016/j.taap.2015.09.029

Table 2.

Site-specific MG modifications in vitro.

Protein Accession Site Peptide Sequence MG-HI (R+54) MG-DH (R+72)
Albumin P02768 R81 LCTVATLRETYGEMADCCAK X X
R117 LVRPEVDVMCTAFHDNEETFLK[K] X X
R186 LDELRDEG[K]ASSAK X X
R218 AWAVARLSQR X X
R257 VHTECCHGDLLECADDRADLAK X X
R410 FQNALLVRYTK X X
R428 [K]VPQVSTPTLVEVSRNLGK X X
R472 TPVSDRVTK X
R445 RMPCAEDYLSVVLNQLCVLHEK X
Serotransferrin P02787 R124 SCHTGLGRSAGWNIPIGLLYCDLPEPR X
Haptoglobin P00738 R41 LRTEGDGVYTLNDK[K] X X
R243 VSVNERVMPICLPS[K]DYAEVGR X
Hemopexin P02790 R185 YYCFQGNQFLRFDPVR X
Ig lambda-2 P0CG05 R83 SHRSYSCQVTHEGSTVEK X
chain C regions

Spectra were identified for the R+54 adduct using human plasma or pure protein incubated with 500 μM MG. Spectra containing the intermediate R+72 dihydroimidazolidine adduct are indicated. All cysteines are carbamidomethylated (C+57) prior to digestion. Brackets indicate alternate cleavage peptides detected.

MG-DH: methylglyoxal-derived dihydroxyimidazolidine

MG-HI: methylglyoxal-derived hydroimidazolone