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Fig. 2. GMT is precipitated with coatomer. The cleared lysate was prepared from yeast producing the Myc6-tagged protein of interest. The tagged protein was immunoprecipitated with anti-Myc antibody and Protein-A/Sepharose beads. Each sample was separated by SDS-PAGE and analysed by immunoblotting with anti-Myc or anti-Ret2p antibody. The total, unbound and bound fractions were examined for Myc6-GMT (pMAV426; lanes 1-3), Myc6-GMT{Delta}4 (pMAV424; lanes 4-6), Myc6-GMT{Delta}12 (pMAV425; lanes 7-9), GMT-Myc6 (pMA12; lanes 10-12), GMT{Delta}12-Myc6 (pMA50; lanes 13-15) and Anp1p-Myc6 (pSV314; lanes 16-18).





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