Extended Data Fig. 2: Representative protein purifications and enzymatic activities of MPXV and VARV CorePro.
From: Substrate recognition and cleavage mechanism of the monkeypox virus core protease
a, MPXV CorePro eluted at ~13.2 mL on a Superdex 200 increase size-exclusion column, corresponding to a molecular weight between 67–158 kDa. The purity as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was >90%. b, MPXV CorePro cleaved a fluorescent substrate S-G32 derived from the second cleavage site of MPXV protein P25K. c, VARV CorePro is also a dimer and d, cleaves S-G32. AU is the abbreviation for arbitrary unit. The enzymatic activity data were derived from n = 4 biological replicates and are presented as mean values ± s.d.
