alpha-D-Fucosidase activity of human and pig kidney: a property of alpha-D-galactosidase.

α-d-Fucosidase activity was demonstrated in human and pig kidneys. Two forms of α-d-fucosidase were separated by gel filtration on Sephadex G-200. The elution profiles of α-d-fucosidases and α-d-galactosidases were identical upon gel filtration and isoelectric focusing. A comparison of the properties of α-d-fucosidase and α-d-galactosidase from human and pig kidney showed that both activities had similar pH optima and similar thermostability and were inhibited to the same extent by d-fucose, d-galactose, and d-galactono-(1→4)-lactone. These data suggest that the hydrolysis of both α-d-fucoside and α-d-galactoside are catalyzed by the same enzyme, α-d-galactoside (fucoside) hydrolase.