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Proteasomes are molecular machines found in virtually all cells that provide one of the mechanisms for protein turnover. We have analysed the 20S proteasome of Schistosoma mansoni, the first multimeric complex isolated from this helminth parasite. Three chromatographic steps were employed to yield a highly homogeneous preparation. 2‐DE of the purified complex revealed 58 spots, of which 46 could be assigned either an α or a β proteasome signature by MS. Most of the 14 transcripts (7α and 7β) encoded by the parasite genome were represented by multiple spots and we suggest that this diversity is due to PTMs of subunits. For most of the isoforms, variations in pI predominated although alterations in mass were also observed. 2‐DE separations of extracts from infective cercariae and blood‐dwelling adult worms probed by Western blotting, using a human anti‐α subunit antibody, revealed different patterns …