Di Matteo G, Orfeo M A, Romeo G
Biochim Biophys Acta. 1976 Apr 8;429(2):527-37. doi: 10.1016/0005-2744(76)90300-4.
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.
人胎盘α-岩藻糖苷酶（EC 3.2.1.51）已被广泛纯化，并在动力学和结构特性方面进行了部分表征。尽管该酶似乎通过DEAE-纤维素色谱法分离为两种形式，它们的分子量和热稳定性不同，但在储存和/或等电聚焦过程中，两种形式之间会发生相互转化，因此在DEAE-纤维素色谱前后，通过后一种技术揭示的相同活性峰被发现。除血清中外，等电聚焦揭示的活性异质峰在不同组织中显示出可重复的模式，血清中的pI值始终更偏酸性。
