Abstract

The glycoprotein hormone family consists of luteinizing hormone (LH), follicle‐stimulating hormone (FSH), and thyroid‐stimulating hormone (TSH), which are secreted by the pituitary gland in all mammalian species, and chorionic gonadotropin (CG) secreted by placental trophoblast cells in primates and equids. These hormones consists of non‐covalently associated α and β subunits. Within a species, the amino acid sequence of the α subunit is identical across all glycoprotein hormones and is encoded by a single gene. The α/β dimer is the active form of the hormone, and biological specificity is conferred by the β subunit. Also in fish, the duality of gonadotropin hormone (GTH), GTH‐1 (FSH‐like GTH), and GTH‐II (LH‐like GTH) is found in certain teleost. In this study, to understand the fundamental mechanisms involved in teleost reproduction and to prove a broader basis for comparative study of teleost GTHs, we produced tethered rec‐eelFSH protein, the cDNA encoding the full‐length eel FSH β‐subunit (signal sequence of 22 amino acid residues and the mature protein of 105 amino acid residues) was fused with the mature protein (93 amino acids) of eel α‐subunit, immunized and A positive hybridoma was selected by ELISA using eel FSH. Anti‐eel glycoprotein mAbs was purified from culture supernatants by affinity chromatography. Six monoclonal antibodies for eel FSH were produced and 2 clones (#11, #5) of these antibodies were bound with α‐subunit of eel glycoprotein. And the other one (#14) was bound with FSHβ. Recombinant FSHβ/α also produced into the CHO cells. Its molecular weight was about 34 kDa. The deglycosylated rec‐FSHβ/α was about 25 kDa. This mAb can specially recognize eel glycoprotein and may serve as a component of eel glycoprotein ELISA kit. (This work was supported by NFRDI. Eun Bi Seo was supported by a scholarship from the BK21 Plus Program (31Z20130012928). the Ministry of Education, Science and Technology, korea)

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