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Guide To Protein Purification, Volume 463

This document provides a summary of the table of contents for the book "Guide to Protein Purification, Volume 463". The book contains 44 chapters organized into 10 sections that cover various strategies, methods, and techniques for protein purification. Topics include developing purification procedures, using bioinformatics, setting up a laboratory, measuring enzyme activity, concentrating proteins, maintaining stability, expression systems, tagging proteins, fractionation, precipitation, chromatography, electrophoresis, membrane proteins, and characterizing purified proteins. The book provides a comprehensive overview of established and emerging protein purification methods.

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Dawlat Salama
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459 views6 pages

Guide To Protein Purification, Volume 463

This document provides a summary of the table of contents for the book "Guide to Protein Purification, Volume 463". The book contains 44 chapters organized into 10 sections that cover various strategies, methods, and techniques for protein purification. Topics include developing purification procedures, using bioinformatics, setting up a laboratory, measuring enzyme activity, concentrating proteins, maintaining stability, expression systems, tagging proteins, fractionation, precipitation, chromatography, electrophoresis, membrane proteins, and characterizing purified proteins. The book provides a comprehensive overview of established and emerging protein purification methods.

Uploaded by

Dawlat Salama
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as DOCX, PDF, TXT or read online on Scribd
  • Why Purify Enzymes?: This section explores the rationale behind enzyme purification and its importance in scientific research.
  • Strategies and Considerations for Protein Purifications: Covers strategic planning and considerations needed when undertaking protein purification processes.
  • Murray Deutscher and Arthur Kornberg: Authored by Murray Deutscher and Arthur Kornberg, detailing key insights into protein purification advancements.
  • Section I: Developing Purification Procedures: This section delves into methods and strategies essential for developing effective purification procedures.
  • Use of Bioinformatics in Planning a Protein Purification: Analyzes how bioinformatics supports planning and enhancing protein purification.
  • Buffers: Principle and Practice: Explains the principles and practical applications of buffers in protein purification.
  • Setting Up A Laboratory: Guidelines for setting up a laboratory effectively to facilitate protein purification.
  • Richard R. Burgess: Introduction to the contributions and perspectives of Richard R. Burgess in the field of protein purification.
  • James E. Noble and Marc J. A. Bailey: Section focusing on the methodologies promoted by James E. Noble and Marc J. A. Bailey in enzyme activity measurement.
  • James D. Watson: Contributions and influence of James D. Watson in the domain of protein research and expression systems.
  • Section II: General Methods for Handling Proteins and Enzymes: Provides general techniques and methods for efficient handling of proteins and enzymes.
  • Measurement of Enzyme Activity: Covers techniques for accurately measuring enzyme activity during purification processes.
  • Key Features: Outlines key features and benefits of the guide, emphasizing expertise and advances in protein purification.
  • Description: Provides an overview of the guide's content and importance, highlighting updates to existing methods and technologies.

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Guide to Protein Purification, Volume 463


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Table of Contents
1. Why Purify Enzymes?

Murray Deutscher and Arthur Kornberg

Section I: Developing Purification Procedures

2. Strategies and Considerations for Protein Purifications

Stuart Linn

3. Use of Bioinformatics in Planning a Protein Purification

Richard R. Burgess

4. Preparing A Purification Summary Table


Richard R. Burgess

Section II: General Methods for Handling Proteins and Enzymes

5. Setting Up A Laboratory

Murray P. Deutscher

6. Buffers: Principle and Practice

Vincent S. Stoll and John S. Blanchard

7. Measurement of Enzyme Activity

T. K. Harris and M. M. Keshwani

8. Quantitation of Protein

James E. Noble and Marc J. A. Bailey

9. Concentration of Proteins and Removal of Solutes

Jonathan K. Romero, David R. H. Evans and Matthew Westoby

10. Maintaining Protein Stability

Murray P. Deutscher

Section III: Recombinant Protein Expression and Purification

11. Selecting an Appropriate Method for Expressing a Recombinant Protein

William H. Brondyk

12. Bacterial Systems for Production of Heterologous Proteins

Frank R. Collart, Ashley M. Frank and Sarah Zerbs

13. Expression in the Yeast Pichia Pastoris

James M. Cregg, Ilya Tolstorukov, Anasua Kusari, Jay Sunga, Knut Madden and Thomas
Chappell

14. Baculovirus-Insect Cell Expression Systems

Donald L. Jarvis
15. Recombinant Protein Production By Transient Gene Transfer Into Mammalian Cells

Sabine Geisse and Cornelia Fux

16. Tagging For Protein Expression

Arun Malhotra

17. Refolding of Solubilized Inclusion Body Proteins

Richard R. Burgess

Section IV: Preparation of Extracts and Subcellular Fractionation

18. Advances In Preparation of Biological Extracts for Protein Purification

Anthony C. Grabski

19. Isolation of Subcellular Organelles and Structures

Jrg Von Hagen and Uwe Michelsen

Section V: Purification Procedures: Bulk Methods

20. Protein Precipitation Techniques

Richard R. Burgess

21. Affi-Gel Blue for Nucleic Acid Removal and Early Enrichment of Nucleotide Binding
Proteins

Murray P. Deutscher

Section VI: Purification Procedures: Chromatographic Methods

22. Ion Exchange Chromatography

Alois Jungbauer and Rainer Hahn

23. Gel Filtration

Earle Stellwagen

24. Protein Chromatography on Hydroxyapatite Columns

Larry J. Cummings, Mark A. Snyder and Kimberly Brisack


25. Theory and Use of Hydrophobic Interaction Chromatography in Protein Purification
Applications

Justin T. Mccue

Section VII: Purification Procedures: Affininty Methods

26. Affinity Chromatography: General Methods

Marjeta Urh, Dan Simpson and Kate Zhao

27. Immobilized-Metal Affinity Chromatography (IMAC)

Frank Schfer* Helena Block, Barbara Maertens, Anne Spriestersbach, Nicole Brinker,
Jan Kubicek, Roland Fabis And Jrg Labahn

28. Identification, Production, and Use of Polyol-Responsive Monoclonal Antibodies for


Immunoaffinity Chromatography

Nancy E. Thompson, Katherine M. Foley, Elizabeth S. Stalder, And Richard R. Burgess

Section VIII: Purification Procedures: Electrophoretic Methods

29. One-Dimensional Gel Electrophoresis

David E. Garfin

30. Protein Analysis Using High-Resolution Two-Dimensional Polyacrylamide Gel


Electrophoresis and Isoelectric Focusing

Friedman

31. Protein Gel Staining Methods: An Introduction And Overview

Thomas H. Steinberg

32. Elution of Proteins From Gels

Richard R. Burgess

33. Immunodetection By Protein Blotting Performing and Optimizing Western Blots With
An Emphasis on Chemiluminescent Detection

Alice Alegria-Schaffer, Krishna Vattem and Andrew Lodge

Section IX: Purification Procedures: Membrane Proteins And Glycoproteins


34. Detergents: An Overview

Dirk Linke

35. Purification of Membrane Proteins

Sue-Hwa Lin and Guido Guidotti

36. Purification of Recombinant G-Protein-Coupled Receptors

Reinhard Grisshammer

37. Cell-Free Translation Of Integral Membrane Proteins Into Unilamelar Liposomes

Michael A. Goren, Akira Nozawa, Shin-Ichi Makino, Russell L. Wrobel and Brian G.
Fox

Section X: Characterization of Purified Proteins

38. Determination of Protein Purity

David G. Rhodes and Thomas M. Laue

39. Determination of Size, Molecular Weight, and Presence of Subunits

David G. Rhodes, Robert E. Bossio and Thomas M. Laue

40. Identification and Quantification of Protein Posttranslational Modifications

Andrew Link

41. Parallel Methods For Expression And Purification

Scott A. Lesley

42. Techniques To Isolate O2-Sensitive Proteins: [4Fe-4S]-FNR As An Example

Aixin Yan and Patricia J. Kiley

43. Rethinking Your Purification Procedure

Murray Deutscher

44. Important But Little Known (Or Forgotten) Artifacts in Protein Biochemistry

Richard R. Burgess
Description
The 2e of this classic Guide to Protein Purification provides a complete update to existing
methods in the field, reflecting the enormous advances made in the last two decades. In
particular, proteomics, mass spectrometry, and DNA technology have revolutionized the field
since the first editions publication but through all of the advancements, the purification of
proteins is still an indispensable first step in understanding their function. This volume examines
the most reliable, robust methods for researchers in biochemistry, molecular and cell biology,
genetics, pharmacology and biotechnology and sets a standard for best practices in the field. It
relates how these traditional and new cutting-edge methods connect to the explosive
advancements in the field. This "Guide to" gives imminently practical advice to avoid costly
mistakes in choosing a method and brings in perspective from the premier researchers while
presents a comprehensive overview of the field today.

Key Features
Gathers top global authors from industry, medicine, and research fields across a wide
variety of disciplines, including biochemistry, genetics, oncology, pharmacology,
dermatology and immunology
Assembles chapters on both common and less common relevant techniques
Provides robust methods as well as an analysis of the advancements in the field that, for
an individual investigator, can be a demanding and time-consuming process

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