Abstract
Human bi-bi-antennary transferrin (Tf) was partially deglycosylated by subsequently incubating with one or more of the following exoglycosidases: neuraminidase, beta-galactosidase or N-Acetyl-beta-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.
MeSH terms
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Amino Acids / analysis
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Carbohydrate Sequence
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Carbohydrates / analysis
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Carcinoma, Hepatocellular / metabolism
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Carcinoma, Hepatocellular / pathology
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Electrophoresis, Polyacrylamide Gel
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Glycoside Hydrolases / chemistry
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Glycoside Hydrolases / metabolism
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Glycosylation
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Humans
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Iron / metabolism*
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Iron / pharmacokinetics
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Mannose / chemistry
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Mannose / metabolism
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Mannosidases / metabolism
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Molecular Sequence Data
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Molecular Weight
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N-Acetylneuraminic Acid / chemistry
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N-Acetylneuraminic Acid / metabolism
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Polysaccharides / chemistry*
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Polysaccharides / metabolism
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Receptors, Transferrin / metabolism*
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Transferrin / chemistry*
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Transferrin / metabolism*
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Tumor Cells, Cultured
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alpha-Mannosidase
Substances
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Amino Acids
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Carbohydrates
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Polysaccharides
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Receptors, Transferrin
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Transferrin
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Iron
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Glycoside Hydrolases
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Mannosidases
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alpha-Mannosidase
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N-Acetylneuraminic Acid
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Mannose