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Fig. 6. Comparison of binding properties of TRE-3^KCNQ4 and TRE^Prest by EMSA. In vitro translated rat TR ${alpha}$ (rTR ${alpha}$ ) and rTRß shifts [³²P]TRE-3^KCNQ4 (lanes 1,3) as well as [³²P]TRE^Prest (lane 5,7) to two complexes with different electromobility (filled and open arrowheads). The interaction of rTR ${alpha}$ or rTRß with [³²P]TRE3^KCNQ4 is significantly reduced in the presence of an excess of unlabeled TRE-3^KCNQ4 competitor oligomers (lanes 2,4). The same is true for rTR ${alpha}$ or rTRß with [³²P]TRE^Prest by using TRE^Prest as a competitor (lanes 6,8).

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