[Production of recombinant eCG with potent FSH-like activity by site-directed mutagenesis].
Equine chorionic gonadotropin (eCG) and luteinizing hormone (eLH) are encoded by a single gene and have identical peptide portions. They, however, differ in the structures of their attached oligosaccharides, which depend on the sites of their production. Recombinant eCG/LH (rec-eCG/LH) possesses dual LH and FSH activities. Mutant eCG/LH in which Asn 56 of the alpha-subunit was changed to Gln to remove the N-linked oligosaccharide showed complete loss of LH activity, whereas in contrast its FSH activity was more potent than that of the wild-type. Another mutant, which lacked the carboxyterminal portion of the beta-subunit to which O-linked oligosaccharides are attached, showed LH activity similar to that of the wild-type, whereas it had the most potent FSH activity. Thus, the oligosaccharides attached to eCG/LH play differential roles in the expression of biological activity.
Shiota
K
K
University of Tokyo, Japan.
Min
K S
KS
Ogawa
T
T
D000818:Animals; D005640:Follicle Stimulating Hormone / Q000502:physiology*; D006064:Gonadotropins, Equine / Q000737:chemistry* / Q000235:genetics*; D006736:Horses; D006801:Humans; D007986:Luteinizing Hormone / Q000737:chemistry* / Q000235:genetics*; D016297:Mutagenesis, Site-Directed; D009844:Oligosaccharides; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
D006064:Gonadotropins, Equine; D009844:Oligosaccharides; D011994:Recombinant Proteins; D007986:Luteinizing Hormone; D005640:Follicle Stimulating Hormone