Beĭer E M, Kliashchitskiĭ B A, Vidershaĭn G Ia
Biokhimiia. 1979 Nov;44(11):1936-43.
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.
在人肾α-L-岩藻糖苷酶的酶制剂于N-（ε-氨基己酰基）-β-L-岩藻吡喃糖基氨基琼脂糖上进行亲和层析的过程中，该酶的洗脱图谱显示出两个组分，可分别命名为α-L-岩藻糖苷酶A和B。在所使用的缓冲液混合物中不存在叠氮化钠时，其中一个组分（岩藻糖苷酶A）被亲和吸附剂保留，而另一个组分（岩藻糖苷酶B）在相同条件下被吸附；后一组分用含有酶抑制剂——L-岩藻糖的溶液洗脱。酶再层析的数据表明岩藻糖苷酶A和B之间存在平衡，它们对亲和吸附剂的亲和力不同。
