Characterization of tethered equine chorionic gonadotropin and its deglycosylated mutants by ovulation stimulation in mice.

ABSTRACT:

Background

To directly assess the biological role of oligosaccharides in recombinant equine chorionic gonadotropin (rec-eCG) functioning, cDNA encoding the full-length eCGβ-subunit was fused with the mature protein part of the α-subunit, and we examined the expression levels of deglycosylated eCG mutants, the ovulation rate for deglycosylated mutants in C57BL/6 mice.

Results

The characterizations of heterodimeric and tethered mutants were studied following their respective secretions in culture medium, molecular weight and ovulation in vivo. Rec-eCG variants containing mutations at glycosylation sites at Asn82 of the α-subunit (eCGβ/αΔ82) and Asn13 of the β-subunit (eCGβΔ13/α) were not efficiently secreted into the culture medium from transfected cells. Western blot analysis

SUBMITTER: Min KS 

PROVIDER: S-EPMC6692925 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature