Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.

@article{Li2000ProcessingON,
  title={Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.},
  author={Jianjun Li and Janne A Quilty and Milka Popov and Reinhart A. F. Reithmeier},
  journal={The Biochemical journal},
  year={2000},
  volume={349 Pt 1},
  pages={51-7}
}
The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop. Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells contained a high-mannose oligosaccharide. The lack of oligosaccharide processing was not due to retention of AE1… CONTINUE READING

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References

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Effect of band 3 subunit

  • H. M. Van Dort, R. Moriyama, P. S. Low
  • 1998

Functional cell

  • R. Beckmann, J. S. Smythe, D. J. Anstee, M. J. Tanner
  • 1998

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