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2004•Journal of Nanjing University of TechnologyRequires access

Secreted expression of human parethyroid hormone(1-84) in Pichia pastoris

Xu Wang, Shuang Li, Zhibin Liu, Bingfang He

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Abstract

The human parathyroid hormone(PTH) gene was synthesized using preferred codons of Pichia pastoris. The hPTH gene was inserted into expression vector pPIC9K containing AOX1 promoter and α-factor secretion signal sequence.The recombinant plasmid was transformed into Pichia pastoris GS115. The recombinants were isolated by G418 screening method and induced by methanol to express the hPTH. The results of tricine-SDS-PAGE and ELISA analysis showed that the hPTH had been expressed and the immunological activity is equivalent to that of 132 ng/L hPTH.

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What this paper is about

The human parathyroid hormone(PTH) gene was synthesized using preferred codons of Pichia pastoris. The hPTH gene was inserted into expression vector pPIC9K containing AOX1 promoter and α-factor secretion signal sequence.The recombinant plasmid was transformed into Pichia pastoris GS115. The recombinants were isolated by G418 screening method and induced by methanol to express the hPTH. The results of tricine-SDS-PAGE and ELISA analysis showed that the hPTH had been expressed and the immunological activity is equivalent to that of 132 ng/L hPTH.

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Available abstract

The human parathyroid hormone(PTH) gene was synthesized using preferred codons of Pichia pastoris. The hPTH gene was inserted into expression vector pPIC9K containing AOX1 promoter and α-factor secretion signal sequence.The recombinant plasmid was transformed into Pichia pastoris GS115. The recombinants were isolated by G418 screening method and induced by methanol to express the hPTH. The results of tricine-SDS-PAGE and ELISA analysis showed that the hPTH had been expressed and the immunological activity is equivalent to that of 132 ng/L hPTH.

Key concepts: Pichia pastoris, Recombinant DNA, Expression vector, Signal peptide, Molecular biology, Biology, Pichia, Secretion

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