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. Author manuscript; available in PMC: 2019 Mar 15.
Published in final edited form as: Anal Biochem. 2018 Mar 15;545:72–77. doi: 10.1016/j.ab.2018.01.018

Table 1.

Mass spectrometry parameters and calibration of amino acids.

Amino Acid Precursor ion Product ion Retention timea DPb EPb CEb CXPb Linear range r2 LoDc LoQc
(mass) (mass) (min ± SD) (volts) (volts) (volts) (volts) (fmol) (fmol) (fmol)
Lysine and derivatives
Lys 147 84 1.16 ± 0.01 40 10 24 12 20 – 5000 0.995 1.30 4.35
1meK 161 84 1.27 ± 0.02 70 10 23 10 20 – 5000 0.998 0.56 1.85
2meK 175 84 1.39 ± 0.07 70 10 25 10 20 – 5000 0.999 0.51 1.69
3meK 189 84 1.46 ± 0.08 70 10 29 10 20 – 5000 0.999 0.42 1.41
Arginine and derivatives
Arg 175 70 3.27 ± 0.01 60 10 33 10 20 – 5000 0.999 0.20 0.65
1meR 189 70 3.27 ± 0.01 50 10 31 8 20 – 5000 0.999 0.56 1.85
2meR 203 70 3.26 ± 0.01 46 10 33 10 20 – 5000 0.999 0.24 0.80
a

Mean ± SD of eight biological replicates collected over a six-month period

b

DP; declustering potential; EP, entrance potential; CE, collision energy; CSP, collision cell exit potential as optimized by Analyst 1.6.1 software.

c

Limits of detection (LoD) and quantification (LoQ) were extrapolated from linear regression analysis as signal-to-background ratios of 3:1 and 10:1, respectively [30].