Human alpha-fucosidase. Single residual enzymatic form in fucosidosis.
Four major forms of alpha-fucosidase (EC 3.2.1.51) activity were separated by isoelectrofocusing from sera of normal control individuals. All forms shifted towards less acidic pI values after neuraminidase treatment. In two patients affected with fucosidosis, only a single major acidic peak was observed and this was affected to a lesser degree by neuraminidase treatment. The kinetics of heat inactivation of the residual activity found in these two patients showed two decay rates while the controls showed only one rate. These data are considered in relation to the hypothesis of the existence of interconvertible thermolabile and thermostable forms of the enzyme which has been discussed in the preceeding paper. The residual alpha-fucosidase found in patients could be structurally altered so that its ability to form the thermostable higher molecular weight aggregates is impaired.
D000293:Adolescent; D002239:Carbohydrate Metabolism, Inborn Errors / Q000201:enzymology*; D002648:Child; D004186:Disaccharidases / Q000172:deficiency*; D005260:Female; D005347:Fibroblasts / Q000201:enzymology; D005643:Fucose / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000172:deficiency* / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008297:Male; D009439:Neuraminidase; D013696:Temperature; D005644:alpha-L-Fucosidase / Q000172:deficiency* / Q000302:isolation & purification / Q000378:metabolism
D007527:Isoenzymes; D005643:Fucose; D004186:Disaccharidases; D009439:Neuraminidase; D005644:alpha-L-Fucosidase