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Vibrio Cholerae

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Cover of 'Vibrio Cholerae'

Table of Contents

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    Book Overview
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    Chapter 1 Laboratory Culturing Techniques and Maintenance of Vibrio cholerae
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    Chapter 2 Genotypic and Phenotypic Assays to Distinguish Vibrio cholerae Biotype
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    Chapter 3 Preparation of Vibrio cholerae Samples for RNA-seq Analysis
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    Chapter 4 Random Transposon Mutagenesis of Vibrio cholerae
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    Chapter 5 Metabolomics of Vibrio cholerae
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    Chapter 6 Natural Cotransformation and Multiplex Genome Editing by Natural Transformation (MuGENT) of Vibrio cholerae
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    Chapter 7 Chromatin Immunoprecipitation
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    Chapter 8 Fly Models of Vibrio cholerae Infection and Colonization
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    Chapter 9 Danio rerio as a Native Host Model for Understanding Pathophysiology of Vibrio cholerae
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    Chapter 10 Transposon Sequencing of Vibrio cholerae in the Infant Rabbit Model of Cholera
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    Chapter 11 Isolation of Outer Membrane Vesicles Including Their Quantitative and Qualitative Analyses
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    Chapter 12 Utilization of Vibrio cholerae as a Model Organism to Screen Natural Product Libraries for Identification of New Antibiotics
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    Chapter 13 Infant Mouse Model of Vibrio cholerae Infection and Colonization
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    Chapter 14 Methods for Assessments of Collagenolytic Activity of the Vibrio cholerae Extracellular Proteases, Purification of Secreted Collagenase VchC, and Extraction of Type I Collagen from Fish Skin
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    Chapter 15 Proteomics of Vibrio cholerae
Attention for Chapter 15: Proteomics of Vibrio cholerae
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Chapter title
Proteomics of Vibrio cholerae
Chapter number 15
Book title
Vibrio Cholerae
Published in
Methods in molecular biology, January 2018
DOI 10.1007/978-1-4939-8685-9_15
Pubmed ID
Book ISBNs
978-1-4939-8684-2, 978-1-4939-8685-9
Authors

Ryszard A. Zielke

Abstract

Combining high-throughput mass spectrometry with isobaric tags for relative and absolute quantification (iTRAQ) allows for the identification and relative quantification of proteins from multiple samples. Furthermore, low-abundance proteins that are usually not detected can be enriched by using only the relevant fraction of the proteome, e.g., cytoplasmic, membrane proteins, or secreted proteins. Described here is a workflow for isolation and enrichment of secreted and membrane proteins that is compatible with mass spectrometry. Isolated proteins are reduced, alkylated, and digested with trypsin, and obtained peptides are labeled with iTRAQ reagent and separated by strong cation exchange to reduce the complexity. Finally, the peptides are separated by reverse-phase chromatography, spotted on a MALDI target plate, and analyzed by MALDI TOF-TOF.

Mendeley readers

The data shown below were compiled from readership statistics for 2 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 2 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 1 50%
Lecturer 1 50%
Readers by discipline Count As %
Veterinary Science and Veterinary Medicine 1 50%
Medicine and Dentistry 1 50%