Abstract
The ability of actin to form stable polymers is important to many cellular processes. Actin polymerization has been measured by a wide variety of methods. Kerwar and Lehrer (1) were the first to demonstrate tryptophan fluorescence changes upon denaturation and polymerization of actin. We and others have made use of this work in assessing actin denaturation (2–4); however, intrinsic fluorescence has not been exploited as a general means of following actin polymerization. Instead, fluorescent probes such as pyrene attached near the C-terminal end of the actin molecule have been the primary tools for monitoring actin polymerization. This approach has yielded a wealth of information, but the possibility that labeled actin does not exactly reflect the characteristics of native actin always remains.
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Selden, L.A., Kinosian, H.J., Estes, J.E., Gershman, L.C. (1994). Influence of the High Affinity Divalent Cation on Actin Tryptophan Fluorescence. In: Estes, J.E., Higgins, P.J. (eds) Actin. Advances in Experimental Medicine and Biology, vol 358. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2578-3_5
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DOI: https://doi.org/10.1007/978-1-4615-2578-3_5
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