Site-directed mutagenesis defines the individual roles of the glycosylation sites on follicle-stimulating hormone.

@article{Flack1994SitedirectedMD,
  title={Site-directed mutagenesis defines the individual roles of the glycosylation sites on follicle-stimulating hormone.},
  author={Melinda Flack and J{\"u}rg Fr{\"o}hlich and Antoine P Bennet and James N. Anasti and Bruce C. Nisula},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 19},
  pages={14015-20}
}
To determine the specific role of each follicle-stimulating hormone (FSH) oligosaccharide, we mutated Asn to Gln at each glycosylation site (alpha Gln52, alpha Gln78, alpha Gln52-78, beta Gln7, beta Gln24, and beta Gln7-24) to selectively inhibit oligosaccharide attachment. For wild-type and mutant FSH, we determined the binding affinity to homogenized rat Sertoli cells and the signal-transducing activity in cultured rat granulosa cells. The binding affinity of FSH lacking any one of the… CONTINUE READING