The common identity of five glycosidases in human liver.
An enzyme has been isolated from human liver by DEAE-cellulose chromatography and has been shown by competitive substrate inhibition to be capable of hydrolysing synthetic beta-D-galactosides, beta-D-glucosides, beta-D-fucosides, beta-D-xylosides, and alpha-L-arabinosides. Another form of alpha-L-arabinosidase activity elutes with the major beta-D-galactosidase component on DEAE-chromatography, but has a different identity on the basis of its stability at 4 degrees C. Liver samples from patients with Gaucher's disease are deficient in beta-D-fucosidase as well as beta-D-glucosidase activity.
D001667:Binding, Competitive; D002648:Child; D002675:Child, Preschool; D004355:Drug Stability; D005260:Female; D005696:Galactosidases / Q000378:metabolism; D005776:Gaucher Disease / Q000201:enzymology; D005959:Glucosidases / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D013329:Structure-Activity Relationship; D005644:alpha-L-Fucosidase / Q000378:metabolism
D007527:Isoenzymes; D005696:Galactosidases; D005959:Glucosidases; D006026:Glycoside Hydrolases; D005644:alpha-L-Fucosidase