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Identification of multiple metabolic enzymes from mice cochleae tissue using a novel functional proteomics technology.


ABSTRACT: A new type of technology in proteomics was developed in order to separate a complex protein mixture and analyze protein functions systematically. The technology combines the ability of two-dimensional gel electrophoresis (2-DE) to separate proteins with a protein elution plate (PEP) to recover active proteins for functional analysis and mass spectrometry (MS)-based identification. In order to demonstrate the feasibility of this functional proteomics approach, NADH and NADPH-dependent oxidases, major redox enzyme families, were identified from mice cochlear tissue after a specific drug treatment. By comparing the enzymatic activity between mice that were treated with a drug and a control group significant changes were observed. Using MS, five NADH-dependent oxidases were identified that showed highly altered enzymatic activities due to the drug treatment. In essence, the PEP technology allows for a systematic analysis of a large enzyme family from a complex proteome, providing insights in understanding the mechanism of drug treatment.

SUBMITTER: Wang DL 

PROVIDER: S-EPMC4374962 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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Identification of multiple metabolic enzymes from mice cochleae tissue using a novel functional proteomics technology.

Wang David L DL   Li Hui H   Liang Ruqiang R   Bao Jianxin J  

PloS one 20150326 3


A new type of technology in proteomics was developed in order to separate a complex protein mixture and analyze protein functions systematically. The technology combines the ability of two-dimensional gel electrophoresis (2-DE) to separate proteins with a protein elution plate (PEP) to recover active proteins for functional analysis and mass spectrometry (MS)-based identification. In order to demonstrate the feasibility of this functional proteomics approach, NADH and NADPH-dependent oxidases, m  ...[more]

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