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

Journal article

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 unab...

Expand abstract

Authors: Scudder, P; Neville, D; Butters, T; Fleet, G; Dwek, R

• Publication status: Published
• Journal: Journal of biological chemistry
• Volume: 265
• Issue: 27
• Pages: 16472-16477
• Publication date: 1990-09-01
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: Female; Humans; Oligosaccharides; Chromatography, Affinity; Pregnancy; Ligands; Chromatography, Gel; alpha-L-Fucosidase; Carbohydrate Conformation; Molecular Sequence Data; Chromatography, Ion Exchange; Milk, Human; Carbohydrate Sequence; Chromatography, High Pressure Liquid; Seeds; Kinetics