Summary
Lysenin is a pore-forming toxin that binds to sphingomyelin in a distribution-dependent manner. Studies of this interaction revealed the heterogeneous organization of sphingomyelin in biomembranes while investigations with non-toxic lysenin helped elucidate the spatial and functional heterogeneity of lipid rafts. This chapter summarizes the characterization of lysenin and discusses the possible applications and limitations of this newly developed sphingomyelin probe.
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© 2006 Springer-Verlag Tokyo
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Kobayashi, T., Yamaji-Hasegawa, A. (2006). Lysenin: A New Probe for Sphingomyelin. In: Hirabayashi, Y., Igarashi, Y., Merrill, A.H. (eds) Sphingolipid Biology. Springer, Tokyo. https://doi.org/10.1007/4-431-34200-1_37
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DOI: https://doi.org/10.1007/4-431-34200-1_37
Publisher Name: Springer, Tokyo
Print ISBN: 978-4-431-34198-7
Online ISBN: 978-4-431-34200-7
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