Expression and analysis of the glycosylation properties of recombinant human erythropoietin expressed in Pichia pastoris

Teh, Ser Huy and Fong, Mun Yik and Mohamed, Zulqarnain (2011) Expression and analysis of the glycosylation properties of recombinant human erythropoietin expressed in Pichia pastoris. Genetics and Molecular Biology, 34 (3). pp. 464-470. ISSN 1415-4757, DOI https://doi.org/10.1590/S1415-47572011005000022.

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Abstract

The Pichia pastoris expression system was used to produce recombinant human erythropoietin, a protein synthesized by the adult kidney and responsible for the regulation of red blood cell production. The entire recombinant human erythropoietin (rhEPO) gene was constructed using the Splicing by Overlap Extension by PCR (SOE-PCR) technique, cloned and expressed through the secretory pathway of the Pichia expression system. Recombinant erythropoietin was successfully expressed in P. pastoris. The estimated molecular mass of the expressed protein ranged from 32 kDa to 75 kDa, with the variation in size being attributed to the presence of rhEPO glycosylation analogs. A crude functional analysis of the soluble proteins showed that all of the forms were active in vivo.

Item Type:	Article
Funders:	UNSPECIFIED
Additional Information:	Teh, Ser Huy Fong, Mun Yik Mohamed, Zulqarnain
Uncontrolled Keywords:	erythropoietin; glycosylation; Pichia pastoris; SOE-PCR
Subjects:	R Medicine
Divisions:	Faculty of Medicine Faculty of Science > Institute of Biological Sciences Deputy Vice Chancellor (Research & Innovation) Office > Centre for Research in Biotechnology for Agriculture
Depositing User:	Prof. Dr. Mun Yik Fong
Date Deposited:	22 Feb 2012 07:27
Last Modified:	18 Nov 2019 08:15
URI:	http://eprints.um.edu.my/id/eprint/2738

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