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Fig. 7. Purification of a tethering factor from yolk granules. (A) Typical anion exchange column (HQ, BioRad) elution profile. The redissolved ammonium sulfate precipitate of proteins stripped from granules by a KI wash was loaded onto the column. Tethering activity elutes at the central, major peak only. (B) Coomassie Blue-stained SDS gel comparison of the protein constituents of whole yolk granules (Yolk) and the anion exchange fraction enriched in tethering activity (TF). The major yolk protein (MYP), the predominate species of this organelle, is indicated with an asterisk. The seven protein bands characteristic of this fraction are numbered. (C) Enrichment of tethering activity as a function of each purification step, as measured by the semi-quantitative tethering assay. The three fractions assessed are the KI-wash ({diamondsuit}), the ammonium sulfate precipitate ({blacksquare}) and the anion-exchange-enriched fraction ({blacktriangleup}). Error bars indicate s.d. (n=3).





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