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Animal Breeding and Genetics
Asian-Australasian Journal of Animal Sciences 2003;16(4): 498-503.
DOI: https://doi.org/10.5713/ajas.2003.498    Published online January 1, 2003.
Production of Biological Active Single Chain Bovine LH and FSH
K. S. Min, M. H. Kang, J. T. Yoon, H. J. Jin, H. H. Seong, Y. M. Chang, H. J. Chung, S. J. Oh, S. G. Yun, W. K. Chang
Luteinizing hormone as other glycoprotein hormones is characterized by a heterodimeric structure composed a common a-subunit noncovalently linked to a specific b-subunit. The correct conformation of the heterodimer is important for efficient secretion, hormonal-specific post-translational modifications, receptor binding and signal transduction. To determine whether a- and b-subunits can be synthesized as a single polypeptide chain (tethered-bLH and -bFSH) and also display biological activities, the tethered-bLH and -bFSH molecules were constructed and transfected into chinese hamster ovary (CHO-K1) cells. LH and FSH activities were assayed by using the human embryonic kidney (HEK) 293 cells expressing rat LH and FSH receptor genes. The tethered-bLH and -bFSH proteins were efficiently secreted and showed a similar activity to the dimeric bovine LH and FSH a/b wild type and native purified from bovine pituitary. The tethered-molecules can be permit development of potent new analogues that stimulate ovarian development. Taken together, a single-chain analog can also be constructed to include additional hormone-specific bioactive generating potentially efficacious compounds. These data indicate the potentiality of the single chain approach to further investigate structure-function relationships of LH and FSH.
Keywords: Tethered-bLH and -FSH; Biological Activity
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