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. 2003 Dec 18;23(1):23–32. doi: 10.1038/sj.emboj.7600042

Table 2.

Influence of phosphate on MT-activated ATPase and on the unbinding rates of monomeric rat kinesin (rK340) and dimeric rat kinesin (rK430)

Effect of phosphate on MT-activated ATPase rK340
rK430
  kcat (s−1) K(0.5)MT (μM) kcat (s−1) K(0.5)MT (μM)
Control 28.83±2.09 3.87±0.86 47.85±3.07 0.71±0.20
+40 mM KCl 11.09±1.22 11.10±2.59 47.11±3.83 13.67±1.99
+20 mM KPi 16.01±3.81 9.75±6.23 42.84±2.82 3.43±0.72
 
Effect of phosphate on unbinding rates rK340
rK430
 
ATP kmax (s−1)
ADP kmax (s−1)
ATP kmax (s−1)
ADP kmax (s−1)
Control 50.58±1.21 25.78±1.51 33.32±1.51 11.30±0.17
+40 mM KCl 49.36±0.77 23.19±0.65 19.04±0.48 9.56±0.21
+20 mM KPi 40.34±0.41 17.96±1.20 13.31±2.58 3.19±0.37