Citation:
HUO Zhong-Zhong, FENG Liu-Xing, LI Hong-Mei, XIONG Jin-Ping. Absolute Quantification of Beta Amyloid Peptide Based on Sulfur Isotope Dilution Mass Spectrometry[J]. Chinese Journal of Analytical Chemistry,
;2019, 47(12): 1931-1937.
doi:
10.19756/j.issn.0253-3820.191384
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The accurate quantification of β-amyloid peptides was achieved by the accurate measurement of sulfur elements in β-amyloid peptides based on high performance liquid chromatography isotope dilution inductively coupled plasmon mass spectrometry (HPLC-ID-ICPMS). Aβ42 in β-amyloid peptide was separated from impurities by optimizing liquid chromatography conditions, and then the eluent was mixed online with enriched 34S diluent. In view of the influence of enriched 34S diluent on 32S/34S signal strength and sensitivity, the flow rate of 34S diluent was optimized. According to the formula of isotope dilution method and the number of S elements in Aβ42, the content of Aβ42 in β amyloid peptide was (0.763±0.0044) g/g. The linear correlation coefficient was 0.999 within the range of 5-60 μg/g, the detection limit was 140 pg/g, and the quantitative limit was 467 pg/g. The recovery of the Aβ42 was between 98% and 105%, and the relative standard deviation was less than 6%. The measurement result of this sample by amino acid hydrolysis method was (0.768±0.0091) g/g, which was in good consistency with the result by this method.
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