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Influence of transferrin glycans on receptor binding and iron-donation
Authors:P Hoefkens  M.I.E Huijskes-Heins  C.M.H de Jeu-Jaspars  W.L van Noort  H.G van Eijk
Affiliation:(1) Department of Chemical Pathology, Erasmus University, Rotterdam, The Netherlands
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.
Keywords:deglycosylation  iron  transferrin
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