作者: Xiangdong Huo , Yueyong Liu , Xu Wang , Pingkai Ouyang , Zhengdong Niu
DOI: 10.1016/J.PEP.2007.03.016
关键词:
摘要: 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 heterodimer to biologically active. Low-level expression the recombinant bFSH factor that limits its usefulness superovulation treatment for cows. To increase production bFSH, human protein disulfide isomerase (hPDI) was expressed simultaneously in engineered Pichia strains. The secretion characteristics with or without hPDI were examined. co-expression increased 1.56 mg/l culture medium, 6-fold higher when compared control strain carrying gene only. These results may generally applicable other glycoprotein hormones yeast.