Figure 1From: Probing the stability of the “naked” mucin-like domain of human α-dystroglycanPurification of the recombinant α-DG mucin-like domain, α-DG(316–484). α-DG-DG(316–484) purification steps were analysed by 12% SDS-PAGE stained with Coomassie Brilliant Blue R-250 dye. Lane 1, overall cell lysate from E. coli expressing the chimaeric protein Trx-α-DG(316–484); lane 2, purified Trx-α-DG(316–484); lane 3, Trx-α-DG(316–484) upon thrombin cleavage: two upper bands referring to α-DG peptides plus a lower band of Trx are observable; lane 4, purified and concentrated α-DG(316–484). The lower band refers to a processed α-DG(316–461) product that has been characterized by mass spectrometry.Back to article page