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Soluble nucleoplasm from Xenopus GVs was incubated with poly r(G)-coated agarose beads. After washing with increasing salt concentration (A) or tRNA (B), bound coilin was monitored on a Western blot with mAb H1. The binding of coilin to poly r(G) is resistant to high salt and to an excess of tRNA competitor, as is its binding to single-stranded DNA. Mobility of molecular weight markers in kilodaltons.
