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Application of Selected Reaction Monitoring to Highly Multiplexed Targeted Quantitative Proteomics

A Replacement for Western Blot Analysis

  • Book
  • © 2013

Overview

Authors:
  1. Michael Kinter

    1. Oklahoma Medical Research Foundation, Oklahoma City, USA

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    You can also search for this author in PubMed   Google Scholar

  2. Caroline S. Kinter

    1. Oklahoma Medical Resarch Foundation, Oklahoma City, USA

    View author publications

    You can also search for this author in PubMed   Google Scholar

  • Explains both the theoretical and experimental details of the selected reaction monitoring experiment as it is applied to proteins?
  • Describes a new type of quantitative proteomics experiment called selected reaction monitoring
  • Reviews the experiment result of a robust and powerful method to measure the abundance of a protein in complex samples
  • Includes supplementary material: sn.pub/extras

Part of the book series: SpringerBriefs in Systems Biology (BRIEFSBIOSYS)

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Table of contents (6 chapters)

  1. Front Matter

    Pages i-xiii
    Download chapter PDF

  2. Introduction to Quantitative Proteomics

    • Michael Kinter, Caroline S. Kinter
    Pages 1-8

  3. Specificity of Detection Is the Key Attribute of Selected Reaction Monitoring

    • Michael Kinter, Caroline S. Kinter
    Pages 9-13

  4. Designing a Selected Reaction Monitoring Method

    • Michael Kinter, Caroline S. Kinter
    Pages 15-33

  5. Sample Processing

    • Michael Kinter, Caroline S. Kinter
    Pages 35-46

  6. Sample Analysis and Data Processing

    • Michael Kinter, Caroline S. Kinter
    Pages 47-59

  7. Future Directions

    • Michael Kinter, Caroline S. Kinter
    Pages 61-65
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Keywords

About this book

  A key experiment in biomedical research is monitoring the expression of different proteins in order to detect changes that occur in biological systems under different experimental conditions.  The method that is most widely used is the Western blot analysis.  While Western blot is a workhorse in laboratories studying protein expression and has several advantages, it also has a number of significant limitations.  In particular, the method is semi-quantitative with limited dynamic range.  Western blot focuses on a single protein per sample with only a small number of representative samples analyzed in an experiment.  New quantitative tools have been needed for some time to at least supplement, & possibly replace, the Western blot. Mass spectrometric methods have begun to compete with Western blot for routine quantitative analyses of proteins.  One of these methods is based on the tandem mass spectrometry technique of selected reaction monitoring (SRM), which is also called multiple reaction monitoring (MRM).  Selected reaction monitoring is actually an older tandem mass spectrometry technique, first described in the late 70s, that is widely utilized in the quantitative analysis of small molecules like drugs & metabolites.  The use of selected reaction monitoring for the quantitative analysis of proteins has a number of advantages.  Most importantly, it is fundamentally quantitative with a wide dynamic range.  The output of the analysis is a numerical result that can range over several orders of magnitude.  Other advantages include sufficient specificity & sensitivity to detect low abundance proteins in complex mixtures.  Finally, selected reaction monitoring can be multiplexed to allow the quantitative analysis of relatively large numbers of proteins in a single sample in a single experiment.     This Brief will explain both the theoretical & experimental details of the selected reaction monitoring experiment as it is appliedto proteins. ​

Authors and Affiliations

  • Oklahoma Medical Research Foundation, Oklahoma City, USA

    Michael Kinter

  • Oklahoma Medical Resarch Foundation, Oklahoma City, USA

    Caroline S. Kinter

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