Abstract
A method is described which permits the purification of proteins in quantities necessary for physicochemical characterization. The protein to be purified is separated from contaminants by electrophoresis in a number of sodium dodecyl sulfate (SDS)-containing polyacrylamide disc gels. The region of each gel which contains the desired protein band is then cut out and the slices are stacked one above another in a tube. After the protein is electrophoresed from the gel slices into a bed of hydroxylapatite, it is eluted from the hydroxylapatite with 0.5 m sodium phosphate (pH 6.4) containing 0.1% SDS and 1 m m dithiothreitol. Protein recovery is greater than 90%.
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