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KMID : 0900920000240020125
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Korean journal of Animal Reproduction
2000 Volume.24 No. 2 p.125 ~ p.142
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On the Secretion and Functions of Equine Chorionic Gonadotropin
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Min K.-S.
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Abstract
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13). Analysis of a purified preparation of eCG revealed that its beta -subunit consists of 149 amino acids, which was confirmed by the molecular cloning of its cDNA. There seem to be at least four to six, or even as many as 11, O-glycosylation sites on the extended C-tenninal region of the eCG beta-subunit. Interestingly, eCG is a unique member of this family, as it appear to be a single molecule that possesses both LH- and FSH-like activities. Using the cDNA prepared from mRNA extracted from equine placental and pituitary tissues, we cloned the cDNA of eCG alpha- and beta -subunits and eFSH beta -subunit. The mRNA expression of each subunit seems to be independently regulated, which may account for differences in the quantities of alpha - and beta -subunits in the placenta and pituitary. Thus, eCG is a distinct molecule from the view points of its biological function and glycoresidue structures. Recombinant eCGs including the mutants which lack oligosaccharides will be useful tools for analyzing the structure-function relationships of gonadotropins in the horse as well as other species. Similar experiments will also clarify the proposed structure and biological functions for the glycoprotein hormones. These experimental are now possible, and hopefully a resolution of the existing controversy will be forthcoming in the near future.
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KEYWORD
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Equine chorionic gonadotropin, Secretion, Structure, Function
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