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Techniques for the Analysis of Membrane Proteins pp 185–234Cite as

Immunochemical analysis of membrane proteins

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Abstract

Membranes have a deceptively simple appearance when viewed in the electron microscope as profiles of thin sections of cells and organelles or as the inner and outer fracture faces of freeze-fractured membranes. This apparent physical simplicity masks the complexity of the variety of proteins found in the majority of membrane structures, with of course a few notable exceptions such as myelin and bacterial purple (bacteriorhodopsin) membranes with a very restricted complement of proteins. Resolving the complex arrays of membrane proteins, determining their functions and molecular mechanisms of action in situ has been a major challenge to the ingenuity of biochemists and immunochemists for several decades. Peripheral membrane proteins soluble in aqueous media, in contrast to the integral proteins (Singer and Nicolson, 19 72), have been much more amenable to biochemical and immunochemical analysis, as for example erythrocyte membrane spectrin (Marchesi and Steers, 1968; Reynolds and Trayer, 1971) and the F1-ATPases that can be released from the membranes by mild treatments and obtained in detergent-free solutions (Pedersen,19 7 5 ; Downie et al.,19 79). Resolution and purification of the integral proteins as either active enzymes or antigens has been much more of a problem, requiring detergent-dissociation (‘solubilization’) of the membranes by surface-active agents that do not destroy their biological activities and even proteolytic cleavage of hydrophobic polypeptides.

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  1. Milton R. J. Salton
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Editors and Affiliations

  1. Department of Biochemistry, University of Southampton, UK

    C. Ian Ragan

  2. Department of Chemistry, University of Essex, Colchester, UK

    Richard J. Cherry

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© 1986 Chapman and Hall

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Salton, M.R.J. (1986). Immunochemical analysis of membrane proteins. In: Ragan, C.I., Cherry, R.J. (eds) Techniques for the Analysis of Membrane Proteins. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-4085-7_8

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  • DOI: https://doi.org/10.1007/978-94-009-4085-7_8

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