Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10235547 | Process Biochemistry | 2012 | 6 Pages |
Abstract
⺠rGALNS was extracellularly produced in Escherichia coli BL21. ⺠Purified enzyme showed a 0.21 U mgâ1 activity and a production yield of 0.78 mg Lâ1. ⺠rGALNS showed similar temperature and pH stability profiles to mammalian GALNS proteins. ⺠rGALNS was not taken up by culture cells. ⺠Glycosylations seem to be necessary for protein uptake but not for stability.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Angela Mosquera, Alexander RodrÃguez, Carlos Soto, Felice Leonardi, Angela Espejo, Oscar F. Sánchez, Carlos J. Alméciga-DÃaz, Luis A. Barrera,