Influence of transferrin glycans on receptor binding and iron-donation |
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Authors: | P Hoefkens M.I.E Huijskes-Heins C.M.H de Jeu-Jaspars W.L van Noort H.G van Eijk |
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Affiliation: | (1) Department of Chemical Pathology, Erasmus University, Rotterdam, The Netherlands |
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Abstract: | Human bi-bi-antennary transferrin (Tf) was partially deglycosylated by subsequently incubating with one or more of the following exoglycosidases: neuraminidase, β-galactosidase or N-Acetyl-β-D-glucosaminidase. Aglyco-Tf obtained from serum of a patient suffering from the Carbohydrate Deficient Glycoprotein syndrome was isolated. Receptor binding and the Tf and iron uptake capacities of the fully glycosylated-, partially deglycosylated- and aglyco-Tf were compared using the human hepatoma cell line PLC/PRF/5. No difference in binding capacity between the iso-Tf fractions could be demonstrated, however, the Tf and iron uptake capacity of aglyco-Tf was clearly reduced compared with the other Tf fractions. This revised version was published online in November 2006 with corrections to the Cover Date. |
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Keywords: | deglycosylation iron transferrin |
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