Plant polypeptides reversibly glycosylated by UDP-glucose. Possible components of Golgi beta-glucan synthase in pea cells.

@article{Dhugga1991PlantPR,
  title={Plant polypeptides reversibly glycosylated by UDP-glucose. Possible components of Golgi beta-glucan synthase in pea cells.},
  author={Kanwarpal S Dhugga and Peter Ulvskov and S R Gallagher and Peter Martin Ray},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 32},
  pages={21977-84}
}
In pea membranes, UDP[14C]Glc glycosylates a approximately 40-kDa polypeptide doublet. This label rapidly disappears if excess unlabeled UDP-Glc, or UDP, is added, indicating that the glycosylation is reversible, and suggesting that the glycosylated polypeptides might be intermediates in a glycosyl transfer reaction. Glycosylation of the doublet requires a divalent cation, the effective ions being the same (except for Zn2+) as those that activate Golgi-localized beta-glucan synthase (GS-I… CONTINUE READING

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