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. Author manuscript; available in PMC: 2014 Mar 1.
Published in final edited form as: Microb Pathog. 2012 Nov 17;56:40–46. doi: 10.1016/j.micpath.2012.11.006

Figure 2. Recombinantly expressed SP168 and TIGR4 ZmpC are functional.

Figure 2

Recombinant SP168 and TIGR4 ZmpC (rZmpC) were purified under denaturing-renaturing conditions. Following purification, their function was assessed by exposing stratified HCLE cells to equimolar amounts (200 pmole) of both enzymes for 1 h and checking for cleavage of the MUC16 ectodomain. A) The expression and purity of the SP168 and TIGR4 rZmpC were monitored by running samples on a denaturing 7.5% polyacrylamide gel. The lanes labeled ‘Uninduced’ and ‘Induced’ represent fractions of E. coli clones harboring zmpC-expression constructs, before and after induction with L-rhamnose, respectively. Protein standards are indicated in kilodaltons (kDa) on the left of the gel. B) Western blot, using the M11 antibody, showing that the purified SP168 and TIGR4 rZmpC cleave MUC16 from HCLE cells.