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. 2008 Aug 15;47(36):9514–9521. doi: 10.1021/bi800747e

Table 1. ATPase Activity and Motility of Kinesin Derivatives.

graphic file with name bi-2008-00747e_0002.jpg
a

Schematic diagrams of enzyme species present, using the same symbols as in Figure 1.

b

Microtubule-stimulated ATPase specific activity per dimer (rows 1−3) or per monomer (row 4) in 1 mM ATP, 1.2 mg/mL microtubules, 25 °C.

c

In single-molecule bead movement assay at 1:1 enzyme dimer:bead mole ratio, 1 mM ATP, 22−23 °C.

d

Data set included some runs where motor ran off the microtubule end.

e

No motility detected. Value given is the detection limit.

f

Implies that heterodimer specific activity is ∼15 s−1, since the preparation is estimated by gel densitometry to contain ∼35% mutant homodimers, which have negligible activity.

g

Not determined.