Protein Purification
Principles, High Resolution Methods, and Applications
3rd Edition
Will be published approx. on 8. April 2011
Book
Hardback
532 pages
978-0-471-74661-4 (ISBN)
Description
This thoroughly revised and updated third edition provides an overview of the principles and methodology of the most frequently used biochemical separation techniques for proteins used today. Balancing theory, procedures, and applications, it offers professionals and students in biochemistry, organic chemistry, and analytical chemistry quick access to a wide range of important techniques, including:
* Gel filtration and ion exchange chromatography
* Affinity and covalent chromatography
* Reversed phase and hydrophobic interaction chromatography
* Ligands from combinatorial libraries
* Electrophoresis in gels
* Immunoelectrophoresis and capillary electrophoresis
* Two-dimensional electrophoresis in proteomics
* Protein elution and blotting techniques
* Large-scale electrophoresis processes
More details
Series
Edition
3. Auflage
Language
English
Place of publication
New York
United States
Target group
Professional and scholarly
Edition type
New edition
Product notice
sewn/stitched
Cloth over boards
Dimensions
Height: 286 mm
Width: 221 mm
Thickness: 33 mm
Weight
1604 gr
ISBN-13
978-0-471-74661-4 (9780471746614)
Schweitzer Classification
Other editions
Additional editions
E-Book
01/2012
3rd Edition
Wiley
€137.99
Available for download
E-Book
03/2011
3rd Edition
Wiley
€134.99
Available for download
Previous edition
Jan-Christer Janson | Lars Rydén
Protein Purification
Principles, High Resolution Methods, and Applications
Book
06/1997
2nd Edition
Wiley
€125.00
Article exhausted; check for reprint
Person
JAN-CHRISTER JANSON is Professor Emeritus at the Department of Physical and Analytical Chemistry, Uppsala University, Uppsala, Sweden.
Content
Preface.
Contributors.
Part I. Introduction.
1.Introduction to Protein Purification (Bo Ersson, Lars Rydén and Jan-Christer Janson).
Part II. Chromatography.
2. Introduction to Chromatography (Jan-Christer Janson and Jan-Åke Jönsson).
3. Gel Filtration (Lars Hagel).
4. Ion Exchange Chromatography (Evert Karlsson and Irwin Hirsh).
5. High-Resolution Reversed-Phase Chromatography (Sylvia Winkel Pettersson).
6. Hydrophobic Interaction Chromatography (Kjell-Ove Eriksson and Makonnen Belew).
7. Immobilized Metal Ion Affinity Chromatography (Lennart Kågedal).
8. Covalent Chromatpgraphy (Francisco Batista-Viera, Lars Rydén and Jan Carlsson).
9. Affinity Chromatography (Francisco Batista-Viera, Jan-Christer Janson and Jan Carlsson).
10. Affinity Ligands from Chemical Combinatorial Libraries (Enrique Carredano and Herbert Baumann).
11. Affinity Ligands from Biological Combinatorial Libraries (Per-Åke Nygren).
Part III. Other Separation Methods and Related Techniques.
12. Membrane Separations (Joachim K. Walter, Zuwei Jin, Maik W. Jornitz and Uwe Gottschalk).
13. Refolding of Inclusion Body Proteins from E. coli (Zhiguo Su, Siannan Lu and Zheng Liu).
14. Purification of PEGylated Proteins (Conan J. Fee and James M. Van Alstine).
Part IV. Electrophoresis.
15. Electrophoresis in Gels (Reiner Westermeier).
16. Conventional Isoelectric Focusing in Gel Slabs and Capillaries and Immobilized pH Gradients (Pier Giorgio Righetti, Alessia Farinazzo, Elisa Fasoli and Sabina Carla Righetti).
17. Two-Dimensional Electrophoresis in Proteomics (Reiner Westermeier and Angelika Görg).
18. Protein Elution and Blotting Techniques (Reiner Westermeier).
19. Capillary Electrophoretic Separations (Wolfgang Thormann).
Part V. Separation Method Optimization.
20. High Throughput Screening Techniques on Protein Purification (Karol M. Lacki and Eggert Brekkan).
Index.