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Whole Gel Eluter Purification of a Functional Multiprotein DNA Replication Complex, Rev A

ved by reversing the polarity of the eluter cell and continuing electrophoresis for 30 seconds at 100 volts. The eluted fractions were harvested, with each fraction containing approximately 500 l of liquid. These fractions were then analyzed by native PAGE and the presence of several enzymatic activities determined in order to assess whether the Whole Gel Eluter could be used for the purification of an intact and functional DNA synthesome.

NATIVE POLYACRYLAMIDE GEL ELECTROPHORESIS, SILVER STAINING
Fifty microliters of the electro-eluted fractions were resolved using a 4% native polyacrylamide gel. SDS was excluded from the gel, running buffer, and sample buffer. The gel was electrophoresed at 90 volts until the dye front reached the bottom of the gel. Following electrophoresis, the gel was silver stained using the Silver Stain Plus kit (Bio-Rad).

DNA POLYMERASE α ASSAY
DNA polymerase α activity was assayed with an activated calf thymus DNA template (Sigma Co.) according to published procedures,2 using [32P]dTTP in place of [3H]dTTP in the assay.

DNA POLYMERASE ASSAY
DNA polymerase activity was detected essentially as described in reference 8, with some modification. The 50 l assay mixture contained 50 ng poly(dA)/oligo(dT) (20:1), 0.25 l [32P]dTTP, 2.5 l core buffer (10 mM MgCl2, 10 M TTP; 25 mM HEPES, pH 5.9, 200 g/ml bovine serum albumin, 5% glycerol). The reaction was carried out at 37 C for 15 minutes and the whole reaction mixture were spotted onto Whatman DE81 filters. The filters were then processed to quantify the amount of radiolabeled nucleotide incorporated into the DNA template.10
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