Abstract
DMPC vesicles were swollen in a buffer containing actin monomers. Protein outside the vesicles was eliminated by enzymatic digestion and ultrafiltration. Polymerization of actin within vesicles was attained by introducing K+ or Mg2+ ions via suitable ionophores. Investigation by DSC showed, that there was no interaction when actin was distributed symmetrically on both sides of the membrane, but that actin interacted well with the lipid when located on one side of the membrane only, with a clear difference between the effects of monomeric and polymeric actin. Microscopic observation and image analysis of thin-walled vesicles demonstrated a correlation between actin polymerization and characteristic shape transitions.
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References
Käs, J., and E. Sackmann, Biophys. J. 60, 1–21 (1991)
Pardee, J.D., and J.A. Spudich, Meth. Enzymol. 85, 164–181 (1982).
MacLean-Fletcher, S., and T.D. Pollard, Biochem.Biophys.Res.Comm. 96, 18–27 (1980).
Detmers, P., et al., J.Biol.Chem. 256, 99–105 (1981).
Cortese, J., et al., Proc.Nat.Acad.Sci.USA 86, 5773–5777 (1989).
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© 1992 Springer-Verlag Berlin Heidelberg
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Bärmann, M., Käs, J., Kurzmeier, H., Sackmann, E. (1992). A New Cell Model — Actin Networks Encaged by Giant Vesicles. In: Lipowsky, R., Richter, D., Kremer, K. (eds) The Structure and Conformation of Amphiphilic Membranes. Springer Proceedings in Physics, vol 66. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-84763-9_26
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DOI: https://doi.org/10.1007/978-3-642-84763-9_26
Publisher Name: Springer, Berlin, Heidelberg
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