Protein Purification.

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Bibliographic Details
Online Access: Full Text (via ProQuest)
Main Author: Bonner, Philip
Format: eBook
Language:English
Published: Milton : Taylor & Francis Group, 2018.
Edition:2nd ed.
Series:BASICS (Garland Science) Ser.
Subjects:
Table of Contents:
  • Cover; Half Title; Title Page; Copyright Page; Table of Contents; Detailed Contents; Preface; Abbreviations; Chapter 1: Water, pH and Buffers; 1.1 Introduction; 1.2 The structure of water; 1.3 Water as a Solvent; 1.4 The Ionisation of Water; 1.5 The pH scale; 1.6 Acids and Bases; 1.7 Buffers; 1.7.1 Points to remember about buffers; 1.8 Summary; Exercise 1.1 Practice calculations using the Henderson-Hasselbalch equation; Recommended Reading; Chapter 2: Protein Structure and Properties; 2.1 Introduction; 2.2 Amino Acids; 2.3 The Peptide Bond; 2.4 Overview of Protein Structure.
  • 2.4.1 Primary structure2.4.2 Secondary structure; 2.4.3 Tertiary structure; 2.4.4 Quaternary structure; 2.5 Motifs and domains (super secondary structure); 2.6 Post-translational Modifications; 2.7 The Characteristics of a Protein Which can be Exploited to Purify a Target Protein; 2.7.1 Surface charge; 2.7.2 Hydrophobic nature; 2.7.3 Solubility; 2.7.4 Biospecificity; 2.7.5 Molecular mass (Mr); 2.7.6 Post-translational modifications; 2.7.7 Engineering proteins to aid purification; 2.8 A range of techniques that can be used in protein purification; 2.8.1 Surface charge; 2.8.2 Hydrophobicity.
  • 2.8.3 Biospecificity2.8.4 Molecular mass; 2.9 Summary; Recommended reading; Chapter 3: Chromatography and the Strategy of Protein Purification; 3.1 Introduction; 3.2 Chromatography; 3.3 The Theories of Chromatography; 3.3.1 The plate theory of chromatography; 3.3.2 The rate theory of chromatography; 3.4 Parameters in Chromatography; 3.5 The Strategy of Protein Purification; 3.5.1 Introduction; 3.5.2 Strategy; 3.5.3 The process of protein purification; 3.6 The Equipment Required for Protein Purification; 3.6.1 Columns; 3.6.2 Tubing; 3.6.3 Pumps; 3.6.4 Fraction collectors; 3.6.5 Detectors.
  • 3.6.6 Gradient makers3.6.7 Different elution procedures; 3.6.7.1 Isocratic elution; 3.6.7.2 Stepped isocratic elution; 3.6.7.3 Gradient elution; 3.6.8 Regeneration and storage of chromatographic resins (media); 3.7 Automated Protein Purification Chromatography Systems; 3.8 Simulated moving bed chromatography (SMBC); 3.9 Protein Purification Chromatographic Runs; 3.9.1 Pre-packed chromatographic columns; 3.9.2 Empty chromatography columns; 3.9.3 Flow rates and elution of the sample; 3.10 Scaling Up the Purification and Some Considerations About Industrial Protein Purification; 3.11 Summary.
  • Protocol for Chapter 3Recommended reading; Chapter 4: The Groundwork; 4.1 Introduction; 4.2 Assay to Identify a Target Protein; 4.2.1 Temperature; 4.2.2 Substrate concentration; 4.2.3 pH; 4.3 Protein Assays; 4.4 The Extraction of Protein from Cells or Tissue; 4.4.1 Introduction; 4.4.2 Reducing agents; 4.4.3 Chelating agents; 4.4.4 Enzyme substrates/Inhibitors/Activators/Cofactors; 4.4.5 Inhibitors of peptidase enzymes; 4.4.6 Phosphatase inhibitors; 4.4.7 Removal of nucleic acids and nucleoproteins; 4.4.8 Removal of lipoproteins; 4.4.9 Additions for the extraction of plant tissue.