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L-Asparaginase from Escherichia Coli II and Erwinia Carotovora Bound to Poly(Methyl Methacrylate)

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Enzyme Engineering Volume 2

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Abstract

The therapeutic use of an immobilized enzyme has several possible advantages over the application of the native enzyme, including 1) the avoidance of toxicity due to a foreign protein, 2) stabilization of enzyme activity, 3) target, rather than systemic application, and 4) greater control of the duration of physiological activity. It is possible that these advantages will more than compensate for the complexity of administration of immobilized enzymes.

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Author information

Authors and Affiliations

  1. Research and Development Laboratories, Corning Glass Works, Corning, New York, USA

    L. S. Hersh

Authors
  1. L. S. Hersh
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Editor information

Editors and Affiliations

  1. Department of Biochemistry, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, 19174, USA

    E. Kendall Pye

  2. Department of Pharmacology, School of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, 15261, USA

    Lemuel B. Wingard Jr.

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© 1974 Plenum Press, New York

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Hersh, L.S. (1974). L-Asparaginase from Escherichia Coli II and Erwinia Carotovora Bound to Poly(Methyl Methacrylate). In: Pye, E.K., Wingard, L.B. (eds) Enzyme Engineering Volume 2. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-8897-9_60

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  • DOI: https://doi.org/10.1007/978-1-4615-8897-9_60

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4615-8899-3

  • Online ISBN: 978-1-4615-8897-9

  • eBook Packages: Springer Book Archive

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