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. 2001 Mar 27;98(7):3762–3767. doi: 10.1073/pnas.071057198

Figure 1.

Figure 1

Purification of RAC. (A) Yeast RAC was purified as described in Materials and Methods. The purification was monitored by SDS/PAGE and staining with Coomassie blue. Lanes represent proteins released from ribosomes by treatment with 700 mM Kacetate (salt wash); the pool of the active fractions after separation of the salt wash on a ResourceQ (resourceQ); the pool of the active fractions after separation on Superdex200 (superdex200); and the pool of the active fractions after separation on MonoQ (monoQ). Molecular mass standards are indicated on the left. (B) Purified RAC is free of Ssb1/2p. Aliquots of the samples shown in A were analyzed by immunoblotting with antibodies specific for Ssz1p, zuotin, and Ssb1/2p.