Gieselmann V, Hasilik A, von Figura K
Hoppe Seylers Z Physiol Chem. 1984 Jun;365(6):651-60. doi: 10.1515/bchm2.1984.365.1.651.
Tartrate-inhibitable acid phosphatase was purified to apparent homogeneity from human placenta. The enzyme is composed of two subunits with an apparent molecular mass of 48 kDa. Each subunit carries one oligosaccharide of the high-mannose/hybride type. The purified enzyme has an isoelectric point of pH 6.2. It cleaves phosphomonoester bonds at acid pH, is competitively inhibited by L-tartrate, Ki = 0.51 microM, and phosphate, Ki = 0.8mM. A monospecific antiserum raised against the purified placental enzyme precipitated 62% and 85% of the tartrate-inhibitable acid phosphatase present in extracts of placenta and fibroblasts, respectively. By means of subcellular fractionation and immunoprecipitation it was shown that the majority of tartrate-inhibitable acid phosphatase is located in lysosomes in normal and mucolipidosis II fibroblasts. In the human Hep G-2 hepatoma cells a significant fraction of the enzyme appears to be associated with non-lysosomal organelles.
酒石酸抑制性酸性磷酸酶从人胎盘中纯化至表观均一。该酶由两个亚基组成，表观分子量为48 kDa。每个亚基携带一个高甘露糖/杂合型寡糖。纯化后的酶的等电点为pH 6.2。它在酸性pH下裂解磷酸单酯键，受到L-酒石酸（Ki = 0.51 microM）和磷酸盐（Ki = 0.8 mM）的竞争性抑制。针对纯化的胎盘酶产生的单特异性抗血清分别沉淀了胎盘和成纤维细胞提取物中62%和85%的酒石酸抑制性酸性磷酸酶。通过亚细胞分级分离和免疫沉淀表明，在正常和成黏脂贮积症II型成纤维细胞中，大部分酒石酸抑制性酸性磷酸酶位于溶酶体中。在人Hep G-2肝癌细胞中，相当一部分该酶似乎与非溶酶体细胞器相关。
