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Purification of Acetylcholinesterase by Covalent Affinity Chromatography

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Immobilized Biochemicals and Affinity Chromatography

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 42))

Abstract

Although the concept of affinity chromatography for the purification of macromolecules goes back many years, it has been only in the last five years or so that the field has blossomed. This development has been fostered by the creation and availability of numerous types of gels for chromatography and by the efforts of a number of highly skillful and imaginative researchers.(1) The standard type of affinity chromatography involves ligands that reversibly bind to the protein with a high degree of specificity. If the protein is an enzyme these ligands are usually selected from reversible inhibitors.

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References

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Author information

Authors and Affiliations

  1. Department of Chemistry, University of Colorado, Boulder, Colorado, 80302, USA

    Houston F. Voss & Irwin B. Wilson

  2. Israel Institute for Biological Research, Ness-Ziona, Israel

    Y. Ashani

Authors
  1. Houston F. Voss
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  2. Y. Ashani
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  3. Irwin B. Wilson
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Editor information

Editors and Affiliations

  1. Department of Chemistry, University of South Carolina, Columbia, South Carolina, USA

    R. Bruce Dunlap

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© 1974 Plenum Press, New York

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Voss, H.F., Ashani, Y., Wilson, I.B. (1974). Purification of Acetylcholinesterase by Covalent Affinity Chromatography. In: Dunlap, R.B. (eds) Immobilized Biochemicals and Affinity Chromatography. Advances in Experimental Medicine and Biology, vol 42. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6982-0_6

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  • DOI: https://doi.org/10.1007/978-1-4684-6982-0_6

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-6984-4

  • Online ISBN: 978-1-4684-6982-0

  • eBook Packages: Springer Book Archive

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