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. Author manuscript; available in PMC: 2012 Apr 15.
Published in final edited form as: J Mol Biol. 2011 Feb 17;407(5):716–730. doi: 10.1016/j.jmb.2011.02.001

Table 4.

Temperature dependence of MV FlAsH actin-activated ATPase activity.

Temperature
(°C)
aV0 bkcat cKATPase dk−pocket
4 0.04 ± 0.04 0.8 ± 0.1 2.5 ± 0.5 0.8 ± 0.1
25 0.08 ± 0.02 6.4 ± 0.3 1.4 ± 0.3 7.7 ± 0.1
35 0.23 ± 0.22 18.8 ± 0.4 2.5 ± 0.2 19.0 ± 0.1
a

ATPase activity in the absence of actin. Errors represent the standard deviation from 3 separate measurements done with three separate protein preparations.

b

Maximum actin-activated ATPase activity determined from fit of data to the Michaelis-Menton relationship. Error bars represent the standard error of the fit of data from three separate protein preparations.

c

Actin concentration at which the ATPase activity is one-half maximal. Error bars represent the standard error of the fit of data from three separate protein preparations.

d

The rate of dmantADP release measured by single turnover (sequential mixing with dmantATP and then actin).