Site-directed mutagenesis defines the individual roles of the glycosylation sites on follicle-stimulating hormone.
作者： M.R. Flack , J. Froehlich , A.P. Bennet , J. Anasti , B.C. Nisula
DOI: 10.1016/S0021-9258(17)36748-0
关键词:
摘要: To determine the specific role of each follicle-stimulating hormone (FSH) oligosaccharide, we mutated Asn to Gln at glycosylation site (alpha Gln52, alpha Gln78, Gln52-78, beta Gln7, Gln24, and Gln7-24) selectively inhibit oligosaccharide attachment. For wild-type mutant FSH, determined binding affinity homogenized rat Sertoli cells signal-transducing activity in cultured granulosa cells. The FSH lacking any one oligosaccharides was increased over while Asn52 Gln52 FSH) markedly reduced, that either (beta Gln7 Gln24 slightly reduced. At site, made a second amino acid substitution Tyr9 Tyr26) an preserved Ser9 Ser26). sequence subunit important for signal transduction, regardless presence or absence oligosaccharide. Thus, has similar impact on affinity, 52 disproportionate Asn24 functions both transduction.
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