Co-expression of human protein disulfide isomerase (hPDI) enhances secretion of bovine follicle-stimulating hormone (bFSH) in Pichia pastoris.

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 1.56 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.

journal_name

Protein Expr Purif

authors

Huo X,Liu Y,Wang X,Ouyang P,Niu Z,Shi Y,Qiu B

doi

10.1016/j.pep.2007.03.016

subject

Has Abstract

pub_date

2007-08-01 00:00:00

pages

234-9

issue

2

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(07)00091-5

journal_volume

54

pub_type

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