Abstract
Acid α-l-fucosidase (EC 3.2.1.51) was obtained from human liver and purified to homogeneity. The enzyme consists of four subunits; each of these has a molecular mass of 50 kDa and bears oneN-linked carbohydrate chain. The structures of these chains were studied at the glycopeptide level by methylation analysis and 500-MHz1H-NMR spectroscopy. Oligomannoside-type chains andN-acetyllactosamine-type chains are present in an approximate ratio of 3∶1. While the oligomannoside-type chains show some heterogeneity in size (Man5–8GlcNAc2), theN-acetyllactosaminetype chains are exclusively bi-α(2–6)-sialyl, bi-antennary in their structure.
These observations on the carbohydrate moieties of α-l-fucosidase substantiate our hypothesis [Overdijket al. (1986) Glycoconjugate J 3:339–50] with respect to the relationship between the oligosaccharide structure of lysosomal enzymes and their residual intracellular activity in I-cell disease. For the series of enzymes examined so far, namely, β-N-acetylhexosaminidase, α-l-fucosidase and β-galactosidase, the relative amount ofN-acetyllactosamine-type carbohydrate increases, while the residual intracellular activity in I-cell disease tissue decreases in this order. The system which is responsible for preferentially retaining hydrolases with (non-phosphorylated) oligomannoside-type chains both in I-cells and in normal cells has yet to be identified.
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Beem, E.P., Lisman, J.J.W., Van Steijn, G.J. et al. Structural analysis of the carbohydrate moieties of α-l-fucosidase from human liver. Glycoconjugate J 4, 33–42 (1987). https://doi.org/10.1007/BF01048442
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DOI: https://doi.org/10.1007/BF01048442