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. 2005 Oct;73(10):6998–7005. doi: 10.1128/IAI.73.10.6998-7005.2005

FIG. 1.

FIG. 1.

Purification of recombinant HCR/A1. (A) BoNT/A1 is cleaved by Clostridial proteases into a dichain toxin that are linked by a disulfide bond. The N-terminal light chain encodes a zinc protease. The C-terminal heavy chain includes a translocation domain (HCT), and a C-terminal receptor binding domain which can be subdivided into an N-terminal (HCRN) and C-terminal domain (denoted ΔA). (B) rHCR/A1 was purified from E. coli cell paste by a three-column strategy. The clarified extract was purified sequentially using nickel affinity, gel filtration and ion exchange chromatography. rHCR/A (5 μg) was separated by SDS-PAGE under reducing conditions and visualized by staining with silver.