2013Journal of Anhui Polytechnic UniversityRequires access

Expression and purification of thymosin α1 in Pichia pastoris

Bin Tang

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Abstract

Thymosin α1(Tα1) was prepared by genetic engineering strain fermentation in this study.The artificial synthesized Tα1 gene was inserted into the pPIC9K plasmid to construct expression vector pPIC9K-Tα1.It was transformed to Pichia pastoris GS115,the recombinant strain was induced by methanol.The supernatant of its fermentation medium was purified by DEAE52 and SephadexG-25.Both Tricine-SDS-PAGE and HPLC indicated that the Tα1 protein was expressed successfully.The expression level was about 4.8 mg/L.

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What this paper is about

Thymosin α1(Tα1) was prepared by genetic engineering strain fermentation in this study.The artificial synthesized Tα1 gene was inserted into the pPIC9K plasmid to construct expression vector pPIC9K-Tα1.It was transformed to Pichia pastoris GS115,the recombinant strain was induced by methanol.The supernatant of its fermentation medium was purified by DEAE52 and SephadexG-25.Both Tricine-SDS-PAGE and HPLC indicated that the Tα1 protein was expressed successfully.The expression level was about 4.8 mg/L.

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Available abstract

Thymosin α1(Tα1) was prepared by genetic engineering strain fermentation in this study.The artificial synthesized Tα1 gene was inserted into the pPIC9K plasmid to construct expression vector pPIC9K-Tα1.It was transformed to Pichia pastoris GS115,the recombinant strain was induced by methanol.The supernatant of its fermentation medium was purified by DEAE52 and SephadexG-25.Both Tricine-SDS-PAGE and HPLC indicated that the Tα1 protein was expressed successfully.The expression level was about 4.8 mg/L.

Key concepts: Pichia pastoris, Recombinant DNA, Expression vector, Fermentation, Pichia, Plasmid, Chemistry, Molecular biology

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