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    Title: Purification and properties of two forms of human α-L-fucosidase
    Authors: Chien, Su-fang;Dawson, Glyn
    Contributors: 淡江大學化學學系
    Date: 1980-01-01
    Issue Date: 2013-05-31 11:34:19 (UTC+8)
    Publisher: Amsterdam: Elsevier BV
    Abstract: High (100 000) and low (50 000) molecular weight forms of α-L-fucosidase (α-fucosidase I and II) were purified to apparent homogeneity from human spleen, liver, brain and kidney on the basis of differential affinity for ε-amino-caproyl fucosamine-agarose bead columns. α-Fucosidase I (the 'bound' form) consisted of two 50 000 dalton monomers; however, both forms can aggregate to tetramer and hexamer forms. Most previous studies on α-fucosidase have been carried out on this form of human α-fucosidase although the bound and unbound forms of the enzyme were present in equal amounts in human spleen. The bound (100 000) form is a sialoglycoprotein whereas the unbound (50 000) form, is a neutral mannose-rich glycoprotein. Other differences with respect to amino acid composition, pH optimum, electrophoretic mobility, K(m), thermal stability, and natural substrate specificities were observed. All preparations hydrolysed 4-methylumbelliferyl-α-L-fucoside, fucosyllactose, and lacto-N-fucopentaose I, but the unbound fraction (α-fucosidase II) preferentially hydrolysed lacto-N-fucopentaose II. The unbound (mannose-rich) α-fucosidase II was taken up by human skin fibroblasts with higher affinity (5% per 2 h per 2.105 cells) than the bound (sialo-) α-fucosidase I (<1% per 2.105 cells). Uptake was inhibited by other lysosomal hydrolases, fetal calf serum, mannose 6-phosphate and phosphomannans and to a lesser extent by heparins. Our studies suggest that α-fucosidase I is not a simple dimer of α-fucosidase II and represents a less-biologically active form of the enzyme.
    Relation: Biochimica Et Biophysica Acta. General Subjects 614(2), pp.476-488
    DOI: 10.1016/0005-2744(80)90237-5
    Appears in Collections:[化學學系暨研究所] 期刊論文

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