| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8328905 | International Journal of Biological Macromolecules | 2018 | 36 Pages |
Abstract
Human thyroid peroxidase (hTPO) has been secretory expressed in AD293 mammalian cells. cDNA sequence of 'Gluc' (Gaussia luciferase) protein from Gaussia princeps was incorporated at the amino terminal of hTPO gene for secretion of targeted protein outside the mammalian cells. Augmentation of TPO clone in serum free mediums was investigated and a simplified purification procedure of hTPO has been reported here. Purified hTPO was further analyzed by SDS-PAGE and immunoblotting (western blotting). The relative molecular mass of hTPO was found to be 105Â kDa. This is the first report with respect to cost effective and simplified purification approach to get highest yield and purity of recombinant hTPO.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Parvinder Kaur, Harshada Patil, Paresh B. Bhanushali, Shamkant B. Badgujar, Anuj Kumar Gupta,