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. 1997 Jul 14;138(1):95–103. doi: 10.1083/jcb.138.1.95

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Purification of ACF2. The peak fractions that contained ACF2 activity after each consecutive purification step (from left to right) were analyzed on 12.5% SDS–polyacrylamide gels. The gels were stained with Coomassie blue and photographed. M, protein molecular weight marker (Life Technologies, Inc., Gaithersburg, MD). E, the starting extract; Q, Q-Sepharose column; AS, 45% ammonium sulfate precipitation; H, heat treatment at 60°C; S, S-Sepharose and heparin columns (connected in series); HI, methyl hydrophobic interaction column; GF, S-200 Gel filtration column; Q2, Bio-Scale Q2 column.

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