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. 2007 Feb 16;189(9):3414–3424. doi: 10.1128/JB.01835-06

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Copyright © 2007, American Society for Microbiology

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FIG. 1. — SDS-PAGE analysis and Western immunoblotting of recombinant GST-mhp379 expressed in E. coli and purified by affinity chromatography. (A) Coomassie brilliant blue-stained gel of recombinant GST-mhp379 (lane U) and thrombin-cleaved recombinant GST-mhp379 (lane C) fusion products separated by SDS-10% PAGE with molecular mass markers (Novex). (B) Western blots of uncleaved (lanes U) and thrombin-cleaved (lanes C) recombinant GST-mhp379 probed with rat antiserum raised against gel-purified thrombin-cleaved recombinant mhp379 (α-mhp379), rabbit antiserum raised against GST (α-GST), rabbit antiserum raised against M. hyopneumoniae strain LKR whole-cell proteins (rabbit α-Mhp), and antiserum from a pig infected with M. hyopneumoniae strain Adelaide Beaufort (pig α-Mhp). Proteins were separated by SDS-10% PAGE with prestained molecular mass markers (New England BioLabs) and Western transferred.