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40
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Text
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URL Address
<a href="http://doi.org/10.1371/journal.pone.0121826" target="_blank" rel="noreferrer noopener">http://doi.org/10.1371/journal.pone.0121826</a>
Rights
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Pages
13-13
Issue
3
Volume
10
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Title
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Identification of Multiple Metabolic Enzymes from Mice Cochleae Tissue Using a Novel Functional Proteomics Technology
Publisher
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PLOS ONE
Date
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2015
2015-03
Subject
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Animal tissues; Beef; Biology; cancer; cancer metabolism; cell metabolism; Cochlea; draft; Drug therapy; E coli; Electrophoresis; Elution; Enzymatic activity; Enzyme assays; Enzyme metabolism; Enzymes; Feasibility studies; Functional analysis; Gel electrophoresis; Genes; Genomics; Hearing impairment; Kinases; Mass spectrometry; Mass spectroscopy; medicine; messenger-rna; metabolism; mice; NAD(P)H oxidase; NADH; Neurobiology; Neurosciences; Nicotinamide adenine dinucleotide; Noise; Otolaryngology; Oxidation-reduction reactions; Phosphatase; Protein expression; proteins; Proteomes; Proteomics; Science & Technology - Other Topics; Sciences: Comprehensive Works; Scientific imaging; Studies; Substance abuse treatment; Technology; United States--US
Creator
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Wang D L; Li H; Liang R Q; Bao J X
Description
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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.
Identifier
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<a href="http://doi.org/10.1371/journal.pone.0121826" target="_blank" rel="noreferrer noopener">10.1371/journal.pone.0121826</a>
Format
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Journal Article
2015
Animal tissues
Bao J X
Beef
Biology
Cancer
cancer metabolism
cell metabolism
Cochlea
draft
Drug Therapy
E coli
Electrophoresis
Elution
Enzymatic activity
Enzyme assays
Enzyme metabolism
Enzymes
Feasibility Studies
Functional analysis
Gel electrophoresis
Genes
Genomics
Hearing impairment
Journal Article
Kinases
Li H
Liang R Q
Mass spectrometry
Mass spectroscopy
Medicine
messenger-rna
Metabolism
Mice
NAD(P)H oxidase
NADH
Neurobiology
Neurosciences
nicotinamide adenine dinucleotide
Noise
otolaryngology
Oxidation-reduction reactions
Phosphatase
PloS one
PROTEIN expression
Proteins
Proteomes
proteomics
Science & Technology - Other Topics
Sciences: Comprehensive Works
Scientific imaging
Studies
Substance abuse treatment
Technology
United States--US
Wang D L