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OA stabilizes different APC substrates. The electrophoretic mobility shift of 35S-labeled Cdc25 caused by activating phosphorylation and the stability of 35S-labeled cyclin B, 35S-labeled Pds1, or 35S-labeled geminin were analyzed in extracts entering mitosis either in the presence (+OA) or absence of 1 μM OA (−OA). Δ90 cyclin was added to all reactions at time zero. Samples were withdrawn at the indicated time points and analyzed by SDS-PAGE and phosphorimaging.
