Mechanisms of glycosylation and sulfation in the Golgi apparatus: evidence for nucleotide sugar/nucleoside monophosphate and nucleotide sulfate/nucleoside monophosphate antiports in the Golgi apparatus membrane.

@article{Capasso1984MechanismsOG,
  title={Mechanisms of glycosylation and sulfation in the Golgi apparatus: evidence for nucleotide sugar/nucleoside monophosphate and nucleotide sulfate/nucleoside monophosphate antiports in the Golgi apparatus membrane.},
  author={Juan M. Capasso and Carlos B. Hirschberg},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1984},
  volume={81 22},
  pages={7051-5}
}
The mechanism of translocation in vitro of sugar nucleotides and adenosine 3'-phosphate 5'-phosphosulfate (PAPS) into the lumen of rat liver Golgi apparatus vesicles has been studied. It has been previously shown that the Golgi apparatus membrane has specific carrier proteins for PAPS and sugar nucleotides. We now report that translocation of the above nucleotide derivatives across Golgi membranes occurs via a coupled equimolar exchange with the corresponding nucleoside monophosphates. An… CONTINUE READING