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新书资源(2008年2月)

Protein purification / Philip L. R. Bonner. — New York : Taylor & Francis, c2007.—(58.17421/B716p)

Contents

    Contents
    
    Abbreviations
    Preface
    Chapter 1 Protein purification strategy and equipment
    1.1 Introduction
    1.2 Reasons to justify the purification of a protein
    1.3 Loss of protein during a purification schedule
    1.4 Overview of protein structure
    1.5 Properties of proteins that enable purification
    1.6 The range of techniques for protein purification
    1.7 Protein purification strategy
    1.8 The process of protein purification
    1.9 The theory of chromatography
    1.10 Equipment required for protein purification
    1.11 Protein purification chromatographic runs
    1.12 Information required for a protein purification balance sheet
    Chapter 2 Groundwork
    2.1 Introduction
    2.2 Acids and bases
    2.3 Buffers
    2.4 Assay to identify a target protein
    2.5 Protein assays
    2.6 Extraction of protein from cells or tissue
    2.7 Techniques used to disrupt tissue or cells
    2.8 Extraction methods for small amounts of tissue or cells
    2.9 Extraction methods for large amounts of animal/plant tissue or cells
    2.10 Extraction methods for bacterial or yeast cells
    2.11 Points to remember about extraction procedures
    2.12 Techniques for clarifying homogenized extracts(centrifugation)
    2.13 Techniques for clarifying homogenized extracts (aqueous two-phase partitioning)
    2.14 Techniques for concentrating proteins from dilute solutions(laboratory scale)
    2.15 Clarification of process-scale extracts
    2.16 Membrane chromatography
    2.17 Storage of protein samples
    Chapter 3 Nonaffinity absorption techniques for purifying proteins
    3.1 Ion exchange chromatography (IEX)
    3.2 Chromatofocusing
    3.3 Hydroxyapatite chromatography
    3.4 Hydrophobic interaction chromatography (HIC)
    3.5 Hydrophobic charge induction chromatography (HCIC)
    3.6 Mixed mode chromatography (MMC)
    Chapter 4 Affinity procedures for purifying proteins
    4.1 Affinity chromatography
    4.2 Covalent chromatography
    4.3 Dye ligand affinity chromatography
    4.4 Immobilized metal (ion) affinity chromatography (IMAC)
    4.5 Immunoaffinity chromatography
    4.6 Lectin affinity chromatography
    4.7 Purification of recombinant proteins
    4.8 IMAC for purifying recombinant proteins
    4.9 Fusion proteins for purifying recombinant proteins
    4.10 Affinity partitioning (precipitation)
    Chapter 5 Nonabsorption techniques for purifying proteins
    5.1 Size exclusion chromatography (SEC)
    5.2 Some factors to consider in SEC
    5.3 Preparation and storage of SEC resins
    5.4 Analytical SEC
    5.5 SEC to separate protein aggregates or the removal of low amounts of contaminating material
    5.6 Desalting (group separation)
    5.7 SEC in the refolding of denatured proteins
    5.8 Preparative polyacrylamide gel electrophoresis (PAGE)
    5.9 Isolation of proteins from polyacrylamide gels or from nitrocellulose membranes
    5.10 Preparative isoelectric focusing (IEF)
    Chapter 6 Monitoring the purity of protein solutions
    6.1 Electrophoresis of proteins
    6.2 The theory of electrophoresis
    6.3 Polyacrylamide gel electrophoresis (PAGE)
    6.4 Western blotting
    6.5 Isoelectric focusing (IEF)
    6.6 Capillary electrophoresis (CE)
    6.7 Reversed phase high-pressure liquid chromatography (RP-HPLC)