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Int J Biol Macromol. 2018 Jan;106:87-94. doi: 10.1016/j.ijbiomac.2017.07.174. Epub 2017 Aug 1.

Purification of recombinant human thyroid peroxidase (hTPO) from AD293 mammalian cells.

Author information

1
Laboratory of Recombinant DNA Technology, Yashraj Biotechnology Ltd., Navi Mumbai 400705, Maharashtra, India.
2
Laboratory of Recombinant DNA Technology, Yashraj Biotechnology Ltd., Navi Mumbai 400705, Maharashtra, India. Electronic address: sham83badgujar@gmail.com.

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 105kDa. This is the first report with respect to cost effective and simplified purification approach to get highest yield and purity of recombinant hTPO.

KEYWORDS:

Augmentation; Gaussia luciferase; Recombinant hTPO protein

PMID:
28778521
DOI:
10.1016/j.ijbiomac.2017.07.174
[Indexed for MEDLINE]

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