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Glycoprotein hormones LH, FSH, TSH and chorionic gonadotrophin are heterodimers composed of two non-covalently associated subunits, a common - and a specific β-subunit. A recombinant baculo-virus containing a cDNA encoding the -subunit of rat glycoprotein hormones was constructed. Viral-infected cells expressed, 48 h post infection, 7–10mg immunoreactive -glycopolypeptide/6x10⁸ cells, of which 65·6% was able to associate with native LHβ and formed a biologically active heterodimeric hormone that bound to testicular receptors. The treatment with specific glycanases showed that the recombinant -subunit was produced as two differently glycosylated forms; an M_r 23 000 form which contained exclusively N-linked carbohydrate units and another of M_r 25 000 which appeared to contain additional O-linked carbohydrate. Data demonstrated that the -subunit was expressed by insect cells in a manner similar to that by mammalian pituitary gonadotropes producing both the N- and O-glycosylated forms although only the N-glycosylated -subunit is known to be capable of associating with the β-subunit.

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