Abstract
The goandotropins (GTHs) follicle‐stimulating hormone (GTH1) and luteinizing hormone (GTH11) are produced in the pituitary gland of all vertebrates, including fish species, and they are key regulators of gonadal development and reproduction. In this study, we produced the deglycosylated mutants of rec‐eelGTHll and analyzed their biological activity using eel LH receptor cell lines. In the hormone secretion, the glycosylation site as Asnα56 dosen't affect, while glycosylation sites at Asnα79 and Asnβ10 have a little effect at the hormone expression into the medium. In western blotting analysis, rec‐LH was detected bands of 32 kDa and the molecular weight was decreased about 2–3 kDa in the single glycosylation site mutants. Deglycosylation treatment by PNGase F was decreased to 25 kDa at the molecular weight of all mutants. Oligosaccharides at Asn56 on α subunit and at Asn10 on β subunit are crucial for eelLH biological activity by using cell lines expressing eel LH receptor.Support or Funding InformationThis work was supported by the project “Seeding production of eel, Anguilla japonica by artificial induction of sexual maturation” (R2017003).
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
