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Glycosylation of Erythropoietin Receptor

  • S. Masuda
  • Y. Hisada
  • M. Ueda
  • R. Sasaki

Abstract

The size of the murine erythropoietin (EPO) receptor (EPO-R), 105 kDa, estimated from EPO.EPO-R cross-linked products,is much higher than that, 53 kDa, predicted from EPO-R cDNA. The lectinbinding properties of the solubilized EPO-R suggested that EPO-R was N-glycosylated. To find whether glycosylation of EPO-R accounted for the difference in size, the decrease in size of [125I]EPO•EPO-R cross-linked products by enzymatic deglycosylation was examined. N-glycosylation of EPO-R was at most 10 kDa, not accounting for the difference in size predicted from cDNA and from cross-linked experiments. The possibilities that may cause the difference in receptor size are discussed.

Keywords

Sialic Acid Erythroid Cell Erythropoietin Receptor Fucose Residue Friend Virus 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media Dordrecht 1991

Authors and Affiliations

  • S. Masuda
    • 1
  • Y. Hisada
    • 1
  • M. Ueda
    • 2
  • R. Sasaki
    • 1
  1. 1.Department of Food Science and Technology, Faculty of AgricultureKyoto UniversityKyotoJapan
  2. 2.Research Institute of Life ScienceSnow Brand MilkTochigiJapan

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