Substrate specificity and some properties of free and immobilized animal alpha-L-fucosidase
Beĭer, E.M.; Vidershaĭn GLa
Biokhimiia 42(5): 881-889
1977
ISSN/ISBN: 0320-9725 PMID: 70233 Document Number: 113582
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.