title: [Heterogeneity of alpha-L-fucosidase from human kidney during affinity chromatography].
abstract: During affinity chromatography on N-(epsilon-aminocaproyl)-beta-L-fucopyranosylaminosepharose of the enzyme preparation of alpha-L-fucosidase from human kidney the elution profile of the enzyme revealed two components, which can be designated as alpha-L-fucosidases A and B. In the absence of sodium aside in the buffer mixtures used one of the components (fucosidase A) was retained by an affinity adsorbent, while the other one (fucosidase B) was adsorbed under the same conditions; the latter component was eluted with a solution containing the enzyme inhibitor--L-fucose. Data from the enzyme rechromatography suggest an equilibrium of the fucosidases A and B, which differ in their affinities for the affinity sorbent.
mesh_terms: D002846:Chromatography, Affinity; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification; D008099:Liver / Q000201:enzymology*; D005644:alpha-L-Fucosidase / Q000302:isolation & purification*
chemical_list: D007527:Isoenzymes; D005644:alpha-L-Fucosidase
vernacular_title: Geterogennost' al'fa-L-fukozidazy iz pochki cheloveka pri affinnoĭ khromatografii.