Library Science

A comprehensive collection of essential, time-tested recipes for successful protein fractionation and purification in any experimental circumstance. The protocols give step-by-step instructions on how to select a source for the protein of interest, how to obtain a usable initial extract, how to purify the protein from that extract using both chemical and molecular methods, and how to dry and store the purified protein. Protein Purification Protocols provides all that is needed to design and carry out a successful purification program. It helps both experienced and novice investigators to clarify and define their purification problems and then provides a comprehensive set of tools for a practical solution. Authors Doonan, Shawn

protein-purification.pdf Table of Contents

1. General Strategies (pp. 1-16)
   Doonan, Shawn
2. Preparation of Extracts from Animal Tissues (pp. 17-22)
   Doonan, Shawn
3. Protein Extraction from Plant Tissues (pp. 23-30)
   Shewry, Peter R.; Fido, Roger J.
4. Extraction of Recombinant Protein from Bacteria (pp. 31-38)
   Worrall, D. Margaret
5. Protein Extraction from Fungi (pp. 39-48)
   Bridge, Paul
6. Subcellular Fractionation of Animal Tissues (pp. 49-56)
   Ryan, Norma M.
7. Subcellular Fractionation of Plant Tissues: Isolation of Chloroplasts and Mitochondria from Leaves (pp. 57-68)
   Tobin, Alyson K.
8. The Extraction of Enzymes from Plant Tissues Rich in Phenolic Compounds (pp. 69-80)
   Pierpoint, William S.
9. Avoidance of Proteolysis in Extracts (pp. 81-94)
   Beynon, Robert J.; Oliver, Simon
10. Concentration of Extracts (pp. 95-102)
    Doonan, Shawn
11. Making and Changing Buffers (pp. 103-114)
    Doonan, Shawn
12. Purification and Concentration by Ultrafiltration (pp. 115-134)
    Schratter, Paul
13. Bulk Purification by Fractional Precipitation (pp. 135-144)
    Doonan, Shawn
14. Ion-Exchange Chromatography (pp. 145-150)
    Sheehan, David; FitzGerald, Richard
15. Hydrophobic Interaction Chromatography (pp. 151-156)
    O’Farrell, Paul
16. Affinity Chromatography (pp. 157-168)
    Cutler, Paul
17. Dye-Ligand Affinity Chromatography (pp. 169-176)
    Worrall, D. Margaret
18. Lectin Affinity Chromatography (pp. 177-186)
    West, Iris; Goldring, Owen
19. Immunoaffinity Chromatography (pp. 187-196)
    Jack, George W.; Beer, David J.
20. Immobilized Metal Ion Affinity Chromatography (pp. 197-210)
    Yip, Tai-Tung; Hutchens, T. William
21. Chromatography on Hydroxyapatite (pp. 211-216)
    Doonan, Shawn
22. Affinity Precipitation Methods (pp. 217-238)
    Irwin, Jane A.; Tipton, Keith F.
23. Isoelectric Focusing (pp. 239-248)
    Westermeier, Reiner
24. Chromatofocusing (pp. 249-254)
    Mantle, Timothy J.; Noone, Patricia
25. Size-Exclusion Chromatography (pp. 255-268)
    Cutler, Paul
26. Fast Protein Liquid Chromatography (FPLC) Methods (pp. 269-276)
    Sheehan, David
27. Reversed-Phase Chromatography of Proteins (pp. 277-292)
    Neville, Bill
28. Extraction of Membrane Proteins (pp. 293-304)
    Ohlendieck, Kay
29. Removal of Detergent from Protein Fractions (pp. 305-312)
    Ohlendieck, Kay
30. Purification of Membrane Proteins (pp. 313-322)
    Ohlendieck, Kay
31. Lyophilization of Proteins (pp. 323-338)
    Fagain, Ciaran O
32. Storage of Pure Proteins (pp. 339-356)
    Fagain, Ciaran O
33. Electroelution of Proteins from Polyacrylamide Gels (pp. 357-362)
    Dunn, Michael J.
34. Electroblotting of Proteins from Polyacrylamide Gels (pp. 363-370)
    Dunn, Michael J.
35. High-Performance Electrophoresis Chromatography (pp. 371-380)
    Desnoyers, Serge; Bourassa, Sylvie; Poirier, Guy G.
36. Practical Column Chromatography (pp. 381-396)
    Doonan, Shawn

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