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J. Biol. Chem., Vol. 265, Issue 27, 16472-16477, Sep, 1990

The isolation by ligand affinity chromatography of a novel form of alpha-L-fucosidase from almond

P Scudder, DC Neville, TD Butters, GW Fleet, RA Dwek, TW Rademacher and GS Jacob
Department of Biochemistry, G.D. Searle & Company, University of Oxford, United Kingdom.

An alpha-fucosidase has been extracted from almond meal and purified 163,000-fold to apparent homogeneity using a novel affinity ligand, N- (5-carboxy-1-pentyl)-1,5-dideoxy-1,5-imino-L-fucitol, coupled to Affi- Gel 102. Substrate specificity studies demonstrate that the enzyme hydrolyzes the alpha-fucosidic linkages in Gal(beta 1----3)(Fuc(alpha 1- ---4]GlcNAc(beta 1----3)Gal(beta 1----4)Glc and Gal(beta 1---- 4)(Fuc(alpha 1----3]GlcNAc(beta 1----3)Gal(beta 1----4)Glc at similar rates but is unable to hydrolyze Fuc(alpha 1----2)Gal, Fuc(alpha 1---- 6)GlcNAc, or the synthetic substrate, p-nitrophenyl alpha-L- fucopyranoside. Hence, the enzyme closely resembles an alpha-fucosidase I isolated previously from a commercial preparation of partially purified almond beta-glucosidase (Ogata-Arakawa, M., Muramatsu, T., and Kobata, A. (1977) Arch. Biochem. Biophys. 181, 353-358). However, native and subunit relative molecular masses of 106,000 and 54,000 respectively, different charge and hydrophobicity properties, and the absence of stimulation by NaCl clearly distinguish this enzyme, designated alpha-fucosidase III, from other almond alpha-fucosidases reported previously.
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