Human alpha-fucosidase. Purification and properties.
Human placental alpha-fucosidase (EC 3.2.1.51) has been extensively purified and partially characterized with respect to kinetic and structured properties. Although the enzyme seems to be separated by DEAE-cellulose chromatography in two forms which differ in their molecular weight and thermostability, an interconversion between the two forms takes place during storage and/or electrofocusing so that the same peaks of activity, revealed by the latter technique, are found before and after DEAE-cellulose chrome. The heterogeneous peaks of activity revealed by isoelectrofocusing show a reproducible pattern in the different tissues examined, except in serum where their pI values are consistently more acidic.
D001921:Brain / Q000201:enzymology; D004186:Disaccharidases / Q000378:metabolism*; D004355:Drug Stability; D005260:Female; D006358:Hot Temperature; D006801:Humans; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D046911:Macromolecular Substances; D009206:Myocardium / Q000201:enzymology; D009928:Organ Specificity; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D011489:Protein Denaturation; D005644:alpha-L-Fucosidase / Q000097:blood / Q000302:isolation & purification / Q000378:metabolism*
D046911:Macromolecular Substances; D004186:Disaccharidases; D005644:alpha-L-Fucosidase