. Author manuscript; available in PMC: 2009 Jan 2.

Published in final edited form as: Mol Cell Endocrinol. 2007 Oct 6;280(1-2):47–62. doi: 10.1016/j.mce.2007.09.011

Table 1. Kinetic Constants of ACTR Binding TRβ0-DNA Complexes.

Apparent K_d and B_max values for ACTR binding to TRβ0 complexes on the DR4 (dimers) and consensus rGH (trimers) TREs. Results were obtained as described in Experimental Procedures and for Figure 2. The results of 3 or more assays are shown. Apparent K_d values are in ng coactivator/20 μl reaction and apparent B_max values are expressed as the percent of the original TR/DNA complex supershifted by the coactivator.

	apparent K_d ± S.D.	apparent B_max ± S.D.
Homodimers	15.9 ± 3.91	340 ± 24.1
Homotrimers	4.18 ± 0.73	314 ± 13.0
Heterodimers	384 ± 84.9	103 ± 6.05
Heterotrimers	15.2 ± 2.67	152 ± 6.67