Protein Purification
Principles, High Resolution Methods, and Applications
3rd Edition
Published on 3. January 2012
532 pages
978-1-118-00219-3 (ISBN)
Description
The authoritative guide on protein purification--nowcompletely updated and revised
Since the Second Edition of Protein Purification waspublished in 1998, the sequencing of the human genome and otherdevelopments in bioscience have dramatically changed the landscapeof protein research. This new edition addresses these developments,featuring a wealth of new topics and several chapters rewrittenfrom scratch.
Leading experts in the field cover all major biochemicalseparation methods for proteins in use today, providingprofessionals in biochemistry, organic chemistry, and analyticalchemistry with quick access to the latest techniques. Entirely newor thoroughly revised content includes:
* High-resolution reversed-phase liquid chromatography
* Electrophoresis in gels
* Conventional isoelectric focusing in gel slabs and capillariesand immobilized pH gradients
* Affinity ligands from chemical and biological combinatoriallibraries
* Membrane separations
* Refolding of inclusion body proteins from E. coli
* Purification of PEGylated proteins
* High throughput screening techniques in protein purification
* The history of protein chromatography
More details
Other editions
Additional editions
Book
04/2011
3rd Edition
Wiley
€158.50
Article not available at the moment
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, LarsRydén and Jan-Christer Janson).
Part II. Chromatography.
2. Introduction to Chromatography (Jan-Christer Janson andJan-Åke Jönsson).
3. Gel Filtration (Lars Hagel).
4. Ion Exchange Chromatography (Evert Karlsson and IrwinHirsh).
5. High-Resolution Reversed-Phase Chromatography (Sylvia WinkelPettersson).
6. Hydrophobic Interaction Chromatography (Kjell-Ove Erikssonand Makonnen Belew).
7. Immobilized Metal Ion Affinity Chromatography (LennartKågedal).
8. Covalent Chromatpgraphy (Francisco Batista-Viera, LarsRydén 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 RelatedTechniques.
12. Membrane Separations (Joachim K. Walter, Zuwei Jin, Maik W.Jornitz and Uwe Gottschalk).
13. Refolding of Inclusion Body Proteins from E. coli (ZhiguoSu, Siannan Lu and Zheng Liu).
14. Purification of PEGylated Proteins (Conan J. Fee and JamesM. Van Alstine).
Part IV. Electrophoresis.
15. Electrophoresis in Gels (Reiner Westermeier).
16. Conventional Isoelectric Focusing in Gel Slabs andCapillaries and Immobilized pH Gradients (Pier Giorgio Righetti,Alessia Farinazzo, Elisa Fasoli and Sabina Carla Righetti).
17. Two-Dimensional Electrophoresis in Proteomics (ReinerWestermeier and Angelika Görg).
18. Protein Elution and Blotting Techniques (ReinerWestermeier).
19. Capillary Electrophoretic Separations (WolfgangThormann).
Part V. Separation Method Optimization.
20. High Throughput Screening Techniques on Protein Purification(Karol M. Lacki and Eggert Brekkan).
Index.
