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| Recombinant hPTH(1-34)ab-HSA Fusion Protein Expressed Steadily and Integrally in Saccharomyces cerevisiae |
| LIU Qing-xia1, ZHUGE bin1, FANG Hui-ying1, ZONG Hong1, JIN Jian2, ZHUGE Jian1 |
1. The Key Laboratory of Industrial Biotechnology, Ministry of Education. Research Center of Industrial Microorganisms, School of Biotechnology, Jiangnan University, Wuxi 214122, China;
2. School of Pharmaceutical Science, Jiangnan University, Wuxi 214122, China |
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Abstract Saccharomyces cerevisiae was used as host to express recombinant human parathyroid hormone (PTH)(1-34)ab-human serum albumin (HSA) fusion protein steadily and completely. A genomic DNA fragment, encoding a fusion protein hPTH(1-34)ab-HSA, was fused to α-factor signal peptide gene by PCR, and a recombinant plasmid pYX-α-hPTH(1-34)ab-HSA was constructed. The recombinant plasmid was introduced in S. cerevisiae strain W303 to produce fusion protein. The results of Western blot and N-terminal amino acid sequencing indicated that the fusion protein hPTH(1-34)ab-HSA was expressed steadily and integrally in S.cerevisiae W303-1A. To solve the incompleteness and instability of hPTH(1-34)ab-HSA fusion protein expressed in Pichia pastoris.
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Received: 18 January 2013
Published: 25 June 2013
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