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hNup155, hCG1, and hGle1B form a heterotrimeric complex in vitro. In vitro transcribed-translated [35S]hNup155 was incubated with bacterially expressed/purified GST-hCG1 in the presence (A) or absence (B) of [35S]hGle1B. The bound proteins were isolated with glutathione-Sepharose, eluted, and separated by SDS-PAGE. Proteins were detected by Coomassie staining or autoradiography. Twenty percent of each reaction was analyzed.
