Table 1.

LC/MS/MS analyses of LDL⁻ Apo-B100 protein modifications

Secondary Structure	Peptide	Modified AA	sequence	MSc	charge	XC	Δcn	modification	% modified
α1	276–287	NO2-Tyr276	Y*GMVAQVTQTLK	51	2	2.8	0.4	nitrotyrosine	100 ± 0
α1	580–589	NO2-Trp583	IVQILPW*EQNEQV	30	2	3.0	0.2	nitrotryptophan	49.8 ± 0.6
α1	580–589	HO-Trp583	IVQILPW*EQNEQV	38	2	3.8	0.3	hydroxytryptophan	32.6 ± 1.9
α1	655–669	NO2-Tyr666	IEGNLIFDPNNY*LPK	46	2	3.3	0.4	nitrotyrosine	18.3 ± 0.7
α1	718–732	NO2-Tyr720	ALY*WAVNGQVPDGVSK	49	2	2.4	0.1	nitrotyrosine	29.9 ± 0.07
β1	1101-115	SO3H-Cys1112	ITEVALMGHLSC*DTK	84	2	4.9	0.5	cysteic acid	100 ± 0
α2	2523–2534	NO2-Tyr2524	MY*QMDIQQELQR	36	2	3.0	0.3	nitrotyrosine	87.1 ± 0.2
β2	3137–3148	NO2-Tyr3139	LPY*TIITPPLK	30	2	1.9	0.5	nitrotyrosine	60.2 ± 0.2
β2	3292–3311	NO2-Tyr3295	VPSY*TLILPSLELPVLHVPR	70	2	5.6	0.5	nitrotyrosine	80.4 ± 0.2
β2	3481–3497	NO2-Tyr3489	LSLESLTSY*FSIESSTK	62	2	4.7	0.7	nitrotyrosine	27.1 ± 1.1
β2	3953–3973	HO-Phe3965	DFSAEYEEDGKF*EGLQEWEGK	59	2	2.5	0.5	HO-phenylalanine	92.6 ± 0.9
α3	4133–4145	NO2-Tyr4141	AASGTTGTY*QEWK	46	2	2.7	0.1	nitrotyrosine	81.8±0.1
			Quantification of NO2-Y
			mMoles NO2-Y/(moles Y)
			LDL− = 34.8 ± 1.0
			tLDL = 2.0 ± 0.2
			nLDL = 0.3 ± 0.1

^*Full annotated MS spectra are represented in the order presented in this table in figures 1–12 of the supplemental section