Adler L
Biochim Biophys Acta. 1978 Jan 12;522(1):113-21. doi: 10.1016/0005-2744(78)90327-3.
The molecular weight of a partially purified alkaline phosphatase (orthophosphoric-monoester phosphohydrolase, EC 3.1.3.1) from the halotolerant yeast Debaryomyces hansenii was estimated to 110,000 by gel filtration. The isoelectric point determined by electrofocusing was at approximately pH 4.4. The enzyme had a broad specificity against phosphomonoesters and also attacked some acid anhydrides. Arsenate, molybdate, and orthophosphate acted as competitive inhibitors. Various metal-binding agents inhibited enzyme activity. A zinc addition almost completely reversed the EDTA inhibition. Magnesium stimulated enzyme activity and was required for maintenance of activity at high concentrations of Na+. Increasing glycerol concentration increased the value of the Michaelis constant (Km) and decreased the maximum velocity (V). Solutions equimolar in KCl and NaCl stimulated enzyme activity by increasing V, whereas the Km was almost unaffected by salt concentration. Enzyme extracted from cells cultured at low salinity was indistinguishable from that of cells grown in the presence of 2.7 M NaCl with respect to several criteria.
通过凝胶过滤法估计，来自耐盐酵母汉逊德巴利酵母的部分纯化碱性磷酸酶（正磷酸单酯磷酸水解酶，EC 3.1.3.1）的分子量为110,000。通过等电聚焦测定的等电点约为pH 4.4。该酶对磷酸单酯具有广泛的特异性，并且还能作用于一些酸酐。砷酸盐、钼酸盐和正磷酸盐作为竞争性抑制剂。各种金属结合剂抑制酶活性。添加锌几乎完全逆转了EDTA的抑制作用。镁刺激酶活性，并且在高浓度Na+存在下维持活性是必需的。甘油浓度增加会增加米氏常数（Km）的值并降低最大速度（V）。等摩尔的KCl和NaCl溶液通过增加V来刺激酶活性，而Km几乎不受盐浓度的影响。从低盐度培养的细胞中提取的酶在几个标准方面与在2.7 M NaCl存在下生长的细胞的酶没有区别。
