An efficient method for detecting membrane protein oligomerization and complex using 05SAR‐PAGE

Author:

Huang Liqun1ORCID,Tong Qiong2,Chen Lang2,Zhao Weijing1,Zhang Zeting2,Chai Zhaofei2,Yang Jun2,Li Conggang12,Liu Maili12,Jiang Ling12

Affiliation:

1. Wuhan National Laboratory for Optoelectronics Huazhong University of Science and Technology Wuhan P. R. China

2. Key Laboratory of Magnetic Resonance in Biological System State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics National Center for Magnetic Resonance in Wuhan Innovation Academy for Precision Measurement Science and Technology Chinese Academy of Sciences Wuhan P. R. China

Abstract

AbstractOligomerization is an important feature of proteins, which gives a defined quaternary structure to complete the biological functions. Although frequently observed in membrane proteins, characterizing the oligomerization state remains complicated and time‐consuming. In this study, 0.05% (w/v) sarkosyl‐polyacrylamide gel electrophoresis (05SAR‐PAGE) was used to identify the oligomer states of the membrane proteins CpxA, EnvZ, and Ma‐Mscl with high sensitivity. Furthermore, two‐dimensional electrophoresis (05SAR/sodium dodecyl sulfate–PAGE) combined with western blotting and liquid chromatography–tandem mass spectrometry was successfully applied to study the complex of CpxA/OmpA in cell lysate. The results indicated that 05SAR‐PAGE is an efficient, economical, and practical gel method that can be widely used for the identification of membrane protein oligomerization and the analysis of weak protein interactions.

Funder

National Natural Science Foundation of China

Publisher

Wiley

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