. 2017 Sep 1;4-5:25–33. doi: 10.1016/j.clinms.2017.08.004

Table 1.

Optimized SRM parameters for the selected proteins and peptides.

Protein	Peptide	Rt (min)	Precursor ion m/z (charge)			Fragment ion m/z (type)			DP (V)	CE (V)
Protein	Peptide	Rt (min)	light	heavy		light	heavy		DP (V)	CE (V)
apoA-I	THLAPYSDELR	12.4	651.3	656.3	+2	950.5	960.5	y8⁺	70	31
						879.4	889.4	y7⁺	70	31
						440.2	445.2	y7²⁺	70	34

apoB	FPEVDVLTK	17.1	524.3	528.3	+2	674.4	682.4	y6⁺	60	28
						803.5	811.5	y7⁺	60	24
						450.8	454.8	y8²⁺	60	24
	GFEPTLEALFGK	19.0	654.8	658.8	+2	664.4	672.4	y6⁺	60	29
						975.6	983.6	y9⁺	60	22
						488.3	492.3	y9²⁺	60	24

apoC-I	TPDVSSALDK	11.5	516.8	520.8	+2	620.3	628.3	y6⁺	27	45
						466.2	842.4	y8⁺	24	45
						834.4	470.3	y9²⁺	27	45

apoC-III	GWVTDGFSSLK	17.7	598.8	602.8	+2	953.5	961.5	y9⁺	23	40
						854.4	862.4	y8⁺	23	40
						244.1	244.1	b2⁺	26	50

apoE	SELEEQLTPVAEETR	15.1	865.9	870.9	+2	902.5	912.5	y8⁺	41	70
						801.4	811.4	y7⁺	41	70
						605.3	615.3	y5⁺	41	70
	LGPLVEQGR	12.4	484.8	489.8	+2	588.3	598.3	y5⁺	50	29
						489.2	499.3	y4⁺	50	26
						399.7	404.7	y7²⁺	50	23
	AATVGSLAGQPLQER	13.7	749.4	754.4	+2	898.5	908.5	y8⁺	70	36
						827.4	837.5	y7⁺	90	33
						642.4	652.4	y5⁺	70	33

HSA	DDNPNLPR	9.3	470.8	475.8	+2	272.0	282.0	y2⁺	40	19
						596.2	606.2	y5⁺	40	20
						298.7	303.7	y5²⁺	50	25
	LVNEVTEFAK	14.8	575.3	579.3	+2	694.2	702.2	y6⁺	50	27
						823.4	831.4	y7⁺	50	26
						937.3	945.3	y8⁺	40	25

BGAL	WVGYGQDSR	11.0	534.3	539.3	+2	286.1	286.1	b2⁺	40	22
						782.1	792.1	y7⁺	40	26
						562.1	572.1	y5⁺	40	26
	IDPNAWVER	14.7	550.3	555.3	+2	774.2	784.2	y6⁺	50	31
						871.2	881.2	y7⁺	50	25
						436.1	441.1	y7²⁺	50	22
	GDFQFNISR	16.0	542.3	547.3	+2	262.1	272.1	y2⁺	50	25
						636.0	646.0	y5⁺	50	28
						764.2	774.2	y6⁺	50	28

Rt: Retention time; CE: Collision energy; DP: Declustering potential.

The transitions used for quantification are listed in bold. The stable isotope labeled (heavy) amino acid residues are underlined.