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Difference Gel Electrophoresis

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Cover of 'Difference Gel Electrophoresis'

Table of Contents

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    Book Overview
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    Chapter 1 Two-Dimensional Gel Electrophoresis and 2D-DIGE
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    Chapter 2 Comparative DIGE Proteomics
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    Chapter 3 2D-DIGE and Fluorescence Image Analysis
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    Chapter 4 DIGE Analysis Software and Protein Identification Approaches
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    Chapter 5 Native DIGE: Efficient Tool to Elucidate Protein Interactomes
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    Chapter 6 Comparative Two-Dimensional Fluorescence Gel Electrophoresis
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    Chapter 7 DIGE-Based Phosphoproteomic Analysis
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    Chapter 8 DIGE Saturation Labeling for Scarce Amounts of Protein from Formalin-Fixed Paraffin-Embedded (FFPE) Tissue
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    Chapter 9 Comparative 3-Sample DIGE Analysis of Skeletal Muscles
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    Chapter 10 DIGE Analysis of ProteoMinerTM Fractionated Serum/Plasma Samples
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    Chapter 11 DIGE Analysis of Human Tissues
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    Chapter 12 DIGE Analysis of Animal Tissues
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    Chapter 13 Rapid 2D DIGE Proteomic Analysis of Mouse Liver
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    Chapter 14 Proteomic Analysis of Lung Tissue by DIGE
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    Chapter 15 Comparative Testis Tissue Proteomics Using 2-Dye Versus 3-Dye DIGE Analysis
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    Chapter 16 DIGE Analysis of Fish Tissues
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    Chapter 17 Protein Digestion for DIGE Analysis
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    Chapter 18 Subcellular Fractionation for DIGE-Based Proteomics
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    Chapter 19 DIGE Analysis of Immunodepleted Plasma
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    Chapter 20 Elucidating Cellular Metabolism and Protein Difference Data from DIGE Proteomics Experiments Using Enzyme Assays
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    Chapter 21 Enzyme Assay Methods to Validate DIGE Proteomics Data
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    Chapter 22 Immunoblot Analysis of DIGE-Based Proteomics
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    Chapter 23 Immunofluorescence Microscopy for DIGE-Based Proteomics
Attention for Chapter 17: Protein Digestion for DIGE Analysis
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Chapter title
Protein Digestion for DIGE Analysis
Chapter number 17
Book title
Difference Gel Electrophoresis
Published in
Methods in molecular biology, January 2018
DOI 10.1007/978-1-4939-7268-5_17
Pubmed ID
Book ISBNs
978-1-4939-7267-8, 978-1-4939-7268-5
Authors

Sandra Murphy, Kay Ohlendieck

Abstract

In-gel digestion of protein spots derived from two-dimensional gels and their subsequent identification by mass spectrometry is involved in a multitude of mass spectrometry-driven proteomic experiments, including fluorescence difference gel electrophoresis (DIGE). This type of proteomic methodology has been involved in the establishment of comparative proteome maps and in the identification of differentially expressed proteins and protein isoforms in health and disease. Most in-gel digestion protocols follow a number of common steps including excision of the protein spots of interest, de-staining, reduction and alkylation (for silver-stained gels), dehydration and overnight digestion with the proteolytic enzyme of choice. While trypsin has been a mainstay of peptide digestion for many years, it does have its shortcomings, particularly related to incomplete peptide digestion, and this has led to a rise in popularity for other proteolytic enzymes either used alone or in combination. This chapter discusses the alternative enzymes available and describes the process of in-gel digestion using the enzyme trypsin.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 10 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 10 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 3 30%
Student > Bachelor 2 20%
Researcher 2 20%
Student > Master 1 10%
Student > Doctoral Student 1 10%
Other 0 0%
Unknown 1 10%
Readers by discipline Count As %
Agricultural and Biological Sciences 4 40%
Computer Science 2 20%
Biochemistry, Genetics and Molecular Biology 1 10%
Unknown 3 30%