Production of recombinant eCG with potent FSH-like activity by site- directed mutagenesis

Kunio Shiota, Kwan Sik Min, Tomoya Ogawa*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


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 α-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 β-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.

Original languageEnglish
JournalFolia Pharmacologica Japonica
Issue numberSUPPL. 1
Publication statusPublished - 1997
Externally publishedYes


  • Chorionic gonadotropin
  • ECG
  • Oligosaccharides
  • Recombinant protein

ASJC Scopus subject areas

  • Pharmacology


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