de Araujo P S, Mies V, Miranda O
Biochim Biophys Acta. 1976 Nov 8;452(1):121-30. doi: 10.1016/0005-2744(76)90063-2.
Acid phosphatases (orthophosphoric-monoester phosphohydrolases (acid optimum), EC 3.1.3.2) of low and high molecular weight were separated by Sephadex G-75 filtration from extracts of rat brain, liver and kidney. The proportion of each phosphatase in the extract depends critically on the method employed for homogenate preparation, and no interconversion between high and low molecular weight forms was detected. In extracts obtained from subcellular organelles only high-molecular-weight acid phosphatase was detected, which is of lysosomal origin. Low-molecular-weight acid -phosphatase is restricted to the cell sap. Low- and high-molecular-weight acid phosphatases were characterized by their elution volumes, specific inhibition and activity with two substrates. It is suggested that the distribution pattern found om rat tissues could be common to all eukaryotic cells.
通过葡聚糖凝胶G - 75过滤从大鼠脑、肝和肾的提取物中分离出低分子量和高分子量的酸性磷酸酶（正磷酸单酯磷酸水解酶（最适酸性），EC 3.1.3.2）。提取物中每种磷酸酶的比例严重依赖于用于匀浆制备的方法，并且未检测到高分子量和低分子量形式之间的相互转化。在从亚细胞器获得的提取物中仅检测到高分子量酸性磷酸酶，其起源于溶酶体。低分子量酸性磷酸酶局限于细胞液。通过它们的洗脱体积、特异性抑制以及对两种底物的活性对低分子量和高分子量酸性磷酸酶进行了表征。有人提出，在大鼠组织中发现的这种分布模式可能在所有真核细胞中都很常见。
