Lam K W, Yam L T
Clin Chem. 1977 Jan;23(1):89-94.
A tartrate-resistant acid phosphatase was isolated from a human leukemic spleen by freeze-thawing in saline and purified by repeated chromatography on carboxymethyl-cellulose. The purified enzyme has a molecular weight of 64 000. It catalyzes the hydrolysis of inorganic and organic pyrophosphate as well as the phenolic ester of monoorthophosphate, with optimal activity between pH 5 and 6. However, there is no activity toward mono-orthophosphate esters of aliphatic alcohols. The present data have identified its catalytic function as a pyrophosphatase. However, it has properties different from the pyrophosphatase previously observed in normal animal tissues.
通过在盐水中冻融从人白血病脾脏中分离出一种抗酒石酸酸性磷酸酶，并通过在羧甲基纤维素上反复层析进行纯化。纯化后的酶分子量为64000。它催化无机和有机焦磷酸以及单正磷酸的酚酯水解，在pH 5至6之间具有最佳活性。然而，对脂肪醇的单正磷酸酯没有活性。目前的数据已确定其催化功能为焦磷酸酶。然而，它具有与先前在正常动物组织中观察到的焦磷酸酶不同的特性。
