[Substrate specificity and some properties of free and immobilized animal alpha-L-fucosidase].
The effect of a partially purified preparation of pig kidney alpha-L-fucosidase on some glycoproteins--human and rabbit gamma-globulin, glycoprotein from sheep submaxillary gland and ceruloplasmin--was studied. It was shown that the action of the enzyme of the glycoproteins was not accompanied by a release of fucose. A comparative study of the properties of free and concanavalin A-Sepharose 4B-bound alpha-L-fucosidase was done. The experimental data is indicative of difference in the pH-dependenced and thermostability of these two enzyme forms. It was found that bound alpha-L-fucosidase, similar to the free form, did not split off fucose from the native blood group substances. The data of isoelectric fucosing of alpha-L-fucosidase suggests the existence of enzyme polymorphism.
D000818:Animals; D002570:Ceruloplasmin / Q000378:metabolism; D004186:Disaccharidases / Q000378:metabolism*; D004355:Drug Stability; D004800:Enzymes, Immobilized; D006023:Glycoproteins / Q000378:metabolism; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007668:Kidney / Q000201:enzymology*; D013329:Structure-Activity Relationship; D013363:Submandibular Gland; D013552:Swine; D005644:alpha-L-Fucosidase / Q000378:metabolism*; D005719:gamma-Globulins / Q000378:metabolism
D004800:Enzymes, Immobilized; D006023:Glycoproteins; D005719:gamma-Globulins; D002570:Ceruloplasmin; D004186:Disaccharidases; D005644:alpha-L-Fucosidase
Substratnaia spetsifichnost' i nekotory svoĭstva svobodnoĭ i immobilizovannoĭ alpha-L-fukozidazy zhivotnykh.