Highly Selective Separations in Biotechnology

Highly Selective Separations in Biotechnology edited by G. Street.

Success in meeting the challenge to produce the commercial products anticipated by the exploitation of biological processes depends upon provid­ ing effective separation protocols. Effectiveness can be measured in terms of selectivity, purity, resolution and validatory success. The major processing...

Full description

Saved in:
Bibliographic Details
Corporate Author: SpringerLink (Online service)
Other Authors: Street, G. (Editor)
Format: eBook
Language:English
Published: Dordrecht : Springer Netherlands : Imprint: Springer, 1994.
Edition:1st ed. 1994.
Series:Springer eBook Collection.
Subjects:
Animal anatomy.
Biotechnology.
Biochemistry.
Electronic resources (E-books)
Online Access:Click to view e-book
Holy Cross Note:Loaded electronically.
Electronic access restricted to members of the Holy Cross Community.
Table of Contents:
  • 1 Overview
  • References
  • 2 Affinity precipitation
  • 2.1 Introduction
  • 2.2 Various formats of affinity precipitation
  • 2.3 Heterobifunctional ligands
  • 2.4 Use of macro affinity ligands
  • 2.5 Practical applications of affinity precipitation
  • 2.6 Affinity precipitation by heterobifunctional ligands
  • 2.7 Comparison of affinity precipitation with other affinity techniques
  • 2.8 Conclusions
  • References
  • 3 Membrane-based affinity separation processes
  • 3.1 Introduction
  • 3.2 Chemical and physical feature of the membrane matrix
  • 3.3 Purification protocol
  • 3.4 Ligand coupling
  • 3.5. Stability of active membranes
  • 3.6 Reuse of ligand coupled membranes
  • 3.7 Storage of ligand coupled membranes in buffer
  • 3.8 Ligand leaching
  • 3.9 Efficiency of ligand coupling
  • 3.10 Effect of flow rates on affinity purification of IgG
  • 3.11 Exhaustive purification of antibodies
  • 3.12 Effect of sample recirculation on yields
  • 3.13 Purification of IgG from ascites fluid and serum
  • 3.14 Efficiency in product recovery
  • 3.15 Applications
  • 3.16 Scale-up
  • 3.17 Discussion
  • References
  • 4 Affinity partitioning
  • 4.1 Introduction
  • 4.2 Two-phase systems
  • 4.3 General ways of steering the partitioning
  • 4.4 Affinity partitioning
  • 4.5 Large-scale extractions
  • 4.6 Use of two-phase systems in bioreactors
  • 4.7 Non-protein partitioning
  • 4.8 Alternative types of affinity ligands
  • 4.9 Counter-current distribution
  • 4.10 Conclusions
  • References
  • 5 The use of reverse micelles for the separation of proteins
  • 5.1 Introduction
  • 5.2 Description of reverse micelles
  • 5.3 The reverse micellar extraction method
  • 5.4 Protein distribution between an aqueous and a conjugated reverse micellar phase
  • 5.5 Mass transfer of protein extraction
  • 5.6 Process development
  • 5.7 Examples of reverse micellar applications for protein separation
  • 5.8 Conclusions
  • References
  • 6 The chemistry and engineering of affinity chromatography
  • 6.1 Introduction
  • 6.2 The role of AC in protein purification
  • 6.3 Affinity packings
  • 6.4 Characterization of AC packings
  • 6.5 Modelling and design of affinity chromatography columns
  • 6.6 Notation
  • References
  • 7 Protein fusions as an aid to purification
  • 7.1 Introduction
  • 7.2 Choice of host organism
  • 7.3 Induction of expression
  • 7.4 Solubilisation of recombinant proteins
  • 7.5 Vectors
  • 7.6 Affinity purification
  • 7.7 Thrombin cleavage of fusion proteins
  • 7.8 General discussion
  • References
  • 8 Chiral separations
  • 8.1 Introduction
  • 8.2 Some stereochemical terms
  • 8.3 Chirality and biological systems
  • 8.4 Methods available for chiral separation
  • 8.5 Conclusion
  • References
  • 9 Molecular imprinting—a versatile technique for the preparation of separation materials of predetermined selectivity
  • 9.1 Introduction
  • 9.2 Preparation of molecular imprints
  • 9.3 Recognition in molecularly imprinted polymers
  • 9.4 Application
  • 9.5 Conclusions
  • References.

Similar Items