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. 1997 Apr 1;94(7):2853–2858. doi: 10.1073/pnas.94.7.2853

Table 1.

Binding of 125I-ChTX to α and α+β membranes

Membrane Kd, pM k−1, s−1 k1, M−1·s−1
α 45.14 ± 5.92 (n = 4) 0.0029 (n = 3) 5.5 × 107 (n = 3)
α+β 0.84 ± 0.11 (n = 5) 0.0004 (n = 5) 2.6 × 108 (n = 3)
α/α+β 53.7 7.3 0.21

The equilibrium dissociation constant (Kd) and the rate constants of association (k1) and dissociation (k−1) for 125I-ChTX binding to membranes derived from COS-1 cells transiently transfected with either α or α+β subunits of the maxi-K channel are presented. These values are the average of several different experiments.