Glycosylation of Erythropoietin Receptor
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.
KeywordsSialic Acid Erythroid Cell Erythropoietin Receptor Fucose Residue Friend Virus
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