Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2021354 | Protein Expression and Purification | 2007 | 6 Pages |
Abstract
Bovine follicle-stimulating hormone (bFSH) is a pituitary gonadotropin composed of two non-covalently associated polypeptide subunits, which must be glycosylated, folded, and assembled as a heterodimer to be biologically active. Low-level expression of the recombinant bFSH is the factor that limits its usefulness as a superovulation treatment for cows. To increase the production of recombinant bFSH, human protein disulfide isomerase (hPDI) was expressed simultaneously in engineered Pichia strains. The secretion characteristics of bFSH with or without hPDI were examined. The co-expression of bFSH and hPDI is increased to 1.56Â mg/l of heterodimer in the culture medium, which is 6-fold higher when compared with the control strain carrying the bFSH gene only. These results may be generally applicable to increase the expression of other glycoprotein hormones in yeast.
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Authors
Xiangdong Huo, Yueyong Liu, Xu Wang, Pingkai Ouyang, Zhengdong Niu, Yuhu Shi, Bingsheng Qiu,