Recombinant full-length human cytomegalovirus protease has lower activity than recombinant processed protease domain in purified enzyme and cell-based assays.

@article{Wittwer2002RecombinantFH,
  title={Recombinant full-length human cytomegalovirus protease has lower activity than recombinant processed protease domain in purified enzyme and cell-based assays.},
  author={Arthur John Wittwer and Christy L Funckes-Shippy and Paul J. Hippenmeyer},
  journal={Antiviral research},
  year={2002},
  volume={55 2},
  pages={
          291-306
        }
}
Herpesviruses encode a protease that is essential for virus replication. The protease undergoes cleavage to a processed form during capsid maturation. A recombinant 75 kDa form of the protease from human cytomegalovirus was purified and compared with the recombinant 29 kDa processed form. Modification with an active site titrant suggested that most of each recombinant protease preparation was active (66 and 86%, respectively). Protease activity was compared using a low-molecular weight peptide… CONTINUE READING
BETA