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. 2008 Dec 22;29(5):1202–1211. doi: 10.1128/MCB.01496-08

FIG. 1.

FIG. 1.

Identification and purification of the TbMTr1 complex. (A) Western blot probing alternate fractions of a 2-to-20% sucrose gradient loaded with either purified His-tagged, E. coli-expressed TbMTr1 (rTbMTr1-His) with anti-His antibody (top) or the TbMTr1-HA fusion protein (TbMTr1−/HA) from T. brucei nuclear extracts with monoclonal anti-HA antibody (bottom). Diamonds indicate the following protein standards: soybean trypsin inhibitor (20.1 kDa), bovine serum albumin (67 kDa), lactate dehydrogenase (140 kDa), and catalase (232 kDa). (B) Western blot using peroxidase anti-peroxidase reagent detecting the TbMTr1-PTP fusion protein in whole-cell extracts resolved with a Benchmark prestained molecular mass marker. (C) Colloidal Coomassie stain of SDS-PAGE gel from final purification step of TbMTr1-PTP purification (right lane). Bands are labeled with apparent molecular masses compared to that of the Benchmark protein ladder (left and center lanes) (Invitrogen).