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Biophys J, December 1999, p. 2911-2919, Vol. 77, No. 6
*Department of Chemistry and Biochemistry, University of California-San Diego, La Jolla, California 92093-0365; #Department of Biophysics and Biophysical Chemistry, The Johns Hopkins School of Medicine, Baltimore, Maryland 21205; and §Salk Institute for Biological Studies, La Jolla, California 92037 USA
We measured the lengths of actin filaments formed by
spontaneous polymerization of highly purified actin monomers by
fluorescence microscopy after labeling with rhodamine-phalloidin. The
length distributions are exponential with a mean of ~7 µm (2600 subunits). This length is independent of the initial concentration of
actin monomer, an observation inconsistent with a simple
nucleation-elongation mechanism. However, with the addition of
physically reasonable rates of filament annealing and fragmenting, a
nucleation-elongation mechanism can reproduce the observed average
length of filaments in two types of experiments: 1) filaments formed
from a wide range of highly purified actin monomer concentrations, and
2) filaments formed from 24 µM actin over a range of CapZ concentrations.
Biophys J, December 1999, p. 2911-2919, Vol. 77, No. 6
© 1999 by the Biophysical Society 0006-3495/99/12/2911/09 $2.00
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