Abstract
The S2 cell system was utilized for the production of recombinant luteinizing hormone (LH) and follicle stimulating hormone (FSH) of the channel catfish (Ictalurus punctatus) as C-terminal His-tagged proteins. When expressed individually, the common α-subunit was secreted in abundance but both β-LH and β-FSH were poorly expressed. However, co-expression of the α-subunit with each of the β subunits using a duel promoter vector resulted in the abundant secretion of LH and FSH α/β heterodimers. These recombinant gonadotropins (GtH) were able to stimulate estradiol secretion in an ovarian follicle bioassay and activate recombinant gonadotropin receptors.
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