| 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.
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Authors
Angela Mosquera, Alexander RodrÃguez, Carlos Soto, Felice Leonardi, Angela Espejo, Oscar F. Sánchez, Carlos J. Alméciga-DÃaz, Luis A. Barrera,