Protein purification : principles, high resolution methods, and applications


Protein purification : principles, high resolution methods, and applications

edited by Jan-Christer Janson

(Methods of biochemical analysis / edited by David Glick, v. 54)

Wiley, c2011

3rd ed

  • : hbk

大学図書館所蔵 件 / 27



Includes bibliographical references and index



The authoritative guide on protein purification now completely updated and revised Since the Second Edition of Protein Purification was published in 1998, the sequencing of the human genome and other developments in bioscience have dramatically changed the landscape of protein research. This new edition addresses these developments, featuring a wealth of new topics and several chapters rewritten from scratch. Leading experts in the field cover all major biochemical separation methods for proteins in use today, providing professionals in biochemistry, organic chemistry, and analytical chemistry with quick access to the latest techniques. Entirely new or thoroughly revised content includes: * High-resolution reversed-phase liquid chromatography * Electrophoresis in gels * Conventional isoelectric focusing in gel slabs and capillaries and immobilized pH gradients * Affinity ligands from chemical and biological combinatorial libraries * 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


Preface. Contributors. Part I. Introduction. 1.Introduction to Protein Purification (Bo Ersson, Lars Ryden and Jan-Christer Janson). Part II. Chromatography. 2. Introduction to Chromatography (Jan-Christer Janson and Jan-Ake Jonsson). 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 Kagedal). 8. Covalent Chromatpgraphy (Francisco Batista-Viera, Lars Ryden 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-Ake 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 Gorg). 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.

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  • Methods of biochemical analysis

    edited by David Glick

    John Wiley & Sons c1954-

    v. 1 , v. 2 , v. 3 , v. 4 , v. 5 , v. 6 , v. 7 , v. 8 , v. 9 , v. 10 , v. 11 , v. 12 , v. 13 , v. 14 , v. 15 , v. 16 , v. 17 , v. 18 , v. 19 , v. 20 , v. 21 , v. 22 , v. 23 , v. 24 , v. 25 , v. 26 , v. 27 , v. 28 , v. 29 , v. 30 , v. 31 , v. 32 , v. 33