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Radiation Fragmentation and Inactivation of Membrane Proteins: Interpretation of Data for Normal and Muted Oligomers

  • Conference paper
Lipid Storage Disorders

Part of the book series: NATO ASI Series ((NSSA,volume 150))

  • 111 Accesses

Abstract

Various hydrodynamic methods exist to determine the molecular sizes of soluble or solubilized proteins. When applied to oligomers, some will yield the subunit size such as SDS Polyacrylamide gel electrophoresis (PAGE) and others, the oligomeric size (gel permeation). The radiation inactivation method is unique since it can be applied to the study of the size of membrane proteins in situ.

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Author information

Authors and Affiliations

  1. Section de Génétique Médicale, Hôpital Sainte-Justine, Université de Montréal, Montréal, Canada, H3T 1C5

    Guy Beauregard, Louise Thauvette & Michel Potier

Authors
  1. Guy Beauregard
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  2. Louise Thauvette
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  3. Michel Potier
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Editor information

Editors and Affiliations

  1. Paul Sabatier University, Toulouse, France

    Robert Salvayre  & Louis Douste-Blazy  & 

  2. Hebrew University—Hadassah School of Medicine, Jerusalem, Israel

    Shimon Gatt

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© 1988 Plenum Press, New York

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Beauregard, G., Thauvette, L., Potier, M. (1988). Radiation Fragmentation and Inactivation of Membrane Proteins: Interpretation of Data for Normal and Muted Oligomers. In: Salvayre, R., Douste-Blazy, L., Gatt, S. (eds) Lipid Storage Disorders. NATO ASI Series, vol 150. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1029-7_60

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  • DOI: https://doi.org/10.1007/978-1-4613-1029-7_60

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-8300-3

  • Online ISBN: 978-1-4613-1029-7

  • eBook Packages: Springer Book Archive

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