Stepan J J, Lau K H, Mohan S, Singer F R, Baylink D J
Department of Medicine, Loma Linda University, CA.
Biochem Biophys Res Commun. 1990 Apr 30;168(2):792-800. doi: 10.1016/0006-291x(90)92391-c.
Tartrate-resistant acid phosphatase type-5 was purified to apparent homogeneity from human osteoclastomas by sequential chromatography on CM-Sepharose, Phenyl-Sepharose, concanavalin A-Sepharose, FPLC Superose-12, and FPLC Mono-S. The purification over the original tissue extract was 1167-fold, with a yield of 16%. An identity in the N-terminal amino acid sequence and Mr was found between this enzyme and two type-5 tartrate-resistant acid phosphatases isolated from hairy cell leukemia spleen. However, they appeared to be different as assessed by amino acid composition. In contrast to a previous report, no evidence was found for two subunits of the tartrate-resistant acid phosphatase.
通过在CM-琼脂糖凝胶、苯基-琼脂糖凝胶、伴刀豆球蛋白A-琼脂糖凝胶、快速蛋白质液相色谱Superose-12和快速蛋白质液相色谱Mono-S上依次进行层析，从人骨巨细胞瘤中纯化出了5型抗酒石酸酸性磷酸酶，使其达到表观均一性。相对于原始组织提取物，纯化倍数为1167倍，产率为16%。发现该酶与从毛细胞白血病脾脏中分离出的两种5型抗酒石酸酸性磷酸酶在N端氨基酸序列和相对分子质量上相同。然而，通过氨基酸组成分析，它们似乎有所不同。与之前的一份报告相反，未发现抗酒石酸酸性磷酸酶存在两个亚基的证据。
