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. Author manuscript; available in PMC: 2008 Jan 9.
Published in final edited form as: J Biol Chem. 1999 May 21;274(21):15159–15166. doi: 10.1074/jbc.274.21.15159

Fig. 4. Gel-shift analysis of rtAhR2s and rtARNTb interactions in vitro.

Fig. 4

Equal amounts of in vitro translated rtAhR2α or rtAhR2β proteins were incubated with equal molar amounts of rtARNTb with, or without, 10 nm TCDD. The samples were then incubated with a 32P-labeled oligonucleotide probe derived from a DRE in the rainbow trout CYP1A enhancer. In some lanes a 10-fold molar excess of unlabeled competitor oligonucleotides was also added as indicated. The bound and free oligonucleotides were separated on a native acrylamide gel, and a phosphorimage of the dried gel is shown. The solid arrow indicates the rtAhR2·rtARNTb·DRE complexes. Open arrows indicate positions of nonspecific complexes.