Protein Digestion for Mass Spectrometry

The protein samples were in-gel digested with 10 ng/μl Glu-C. Then, the peptide samples were resuspended in loading buffer (0.03% trifluoroacetic acid, 0.1% formic acid, and 1% acetonitrile), then loaded onto a 20-cm nano-HPLC column and finally generated by a Dionex RSLCnano UPLC system (Thermo, USA). Peptides were ionized with 2.0 kV electrospray ionization voltage from a nano-ESI source on an Orbitrap Fusion mass spectrometer (Thermo, USA) [28 (link)].

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Lei K., Gu X., Alvarado A.G., Du Y., Luo S., Ahn E.H., Kang S.S., Ji B., Liu X., Mao H., Fu H., Kornblum H.I., Jin L., Li H, & Ye K. (2020). Discovery of a dual inhibitor of NQO1 and GSTP1 for treating glioblastoma. Journal of Hematology & Oncology, 13, 141.

Publication 2020

Dionex RSLCnano UPLC system

Acetonitrile Buffer Formic acid Hplc Peptides Protein Trifluoroacetic acid

Corresponding Organization : Shenyang Pharmaceutical University

Other organizations : Emory University, Huazhong University of Science and Technology, Tongji University, Tongji Hospital

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Variable analysis

independent variables

Glu-C enzyme concentration (10 ng/μl)

dependent variables

Peptide samples generated

control variables

Loading buffer (0.03% trifluoroacetic acid, 0.1% formic acid, and 1% acetonitrile)
20-cm nano-HPLC column
Dionex RSLCnano UPLC system
Electrospray ionization voltage (2.0 kV)
Nano-ESI source
Orbitrap Fusion mass spectrometer

controls

No positive or negative controls were explicitly mentioned in the provided information.

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