Citation: KOU Wei, ZHANG Hua, KONSTANTIN Chingin, CHEN Huan-Wen. Charged Bubble Extractive Ionization Mass Spectrometry for Protein Analysis[J]. Chinese Journal of Analytical Chemistry, ;2017, 45(12): 1937-1943. doi: 10.11895/j.issn.0253-3820.171358 shu

Charged Bubble Extractive Ionization Mass Spectrometry for Protein Analysis

1.
State Key Laboratory of Inorganic Synthesis and Preparative Chemistry, Jilin University, Changchun 130012, China
2.
Jiangxi Key Laboratory for Mass Spectrometry and Instrumentation, East China Institute of Technology, Nanchang 330013, China

Corresponding author: CHEN Huan-Wen, chw8868@gmail.com
Received Date: 20 October 2017
Accepted Date: 8 November 2017

Fund Project: Science and Technology Planning Project at the Minitry of Science and Technology of Jiangxi Province 20151BBG70038the National Natural Science Foundation of China 21427802International Science & Technology Cooperation Program of China 2015DFA40290This work was supported by the National Natural Science Foundation of China (No. 21427802), International Science & Technology Cooperation Program of China (No.2015DFA40290), Science and Technology Planning Project at the Minitry of Science and Technology of Jiangxi Province (No. 20151BBG70038)

Figures(6)

Rapid mass spectrometry analysis of protein in the solution sample was carried out by using a charged bubble extraction ionization device. In this work, experimental parameters including gases (N₂ and CO₂), bubble path length, voltage, and gas pressure on the charged bubble extraction ionization of lysozyme were investigated. Under the optimum experimental parameters including CO₂ as extraction gas, bubble path length of 32 cm, solution voltage of 2 kV and gas pressure of 0.05 MPa, this method was successfully used for the protein detection with the limits of detection of 1×10^-8 mol/L in water solution and 1×10^-7 mol/L in diluted urine (200 times in ultrapure water). In addition, the limit of detection of 1×10^-5 mol/L in undiluted urine was obtained with a urine volume of 6 mL at 2 kV voltage and 0.06 MPa gas pressure. By comparing the desalting effects in charged bubble extractive ionization mass spectrometry and ESI-MS, it was found that the bubble charged extraction ionization method could obtain a wider and lower charge state distribution of protein ions, and had higher tolerance ability when facing non-volatile inorganic salts. Off-line study of the collected catalase after charged bubble extraction showed that 53.9% enzyme activity was remained, which indicated that the proposed method was a soft ionization method. The method had merits including no sample pretreatment, no chemical reagent contamination and high speed, showing potential application to mass spectrometry analysis of protein components in solution. Therefore, this study provided a new method for mass spectrometry analysis of biological protein samples.
- Protein sample,
- Bubble,
- Charged bubble extractive ionization,
- Mass spectrometry
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沈阳化工大学材料科学与工程学院沈阳 110142