Chambers J P, Peters S P, Glew R H, Lee R E, McCafferty L R, Mercer D W, Wenger D A
Metabolism. 1978 Jul;27(7):801-14. doi: 10.1016/0026-0495(78)90215-9.
Although the primary genetic defect in all individuals with Gaucher's disease is a deficiency in glucocerebrosidase activity, the finding of marked elevations in splenic and serum acid phosphatase activity is almost as consistent a finding. Gaucher spleen and serum contain at least two forms of acid phosphatase that can be readily separated by chromatography on columns containing the cation exchange resin Sulphopropyl Sephadex. The major species of acid phosphatase (designated SP-I) contained in Triton X-100 (1% v/v) extracts of Gaucher spleen accounts for 65%--95% of the total activity and has the following properties: (1) it does not bind to the cation exchange column; (2) it exhibitis a pH optimum of 4.5--5.0; (3) it is inhibited by sodium fluoride (15 mM), L(+)-tartaric acid (20 mM), and beta-mercaptoethanol (2.1 M), and (4) it is resistant to inhibition by sodium dithionite (10 mM). The minor acid phosphatase activity (designated SP-II) present in extracts of Gaucher spleen has properties similar to those of the major species of acid phosphatase activity contained in serum from patients with Gaucher's disease: (1) it binds firmly to cation exchange columns (eluted by 0.5 M sodium chloride); (2) it exhibits a pH optimum of 5.0--6.0; (3) it is inhibited by sodium fluoride and sodium dithionite; and (4) it is resistant to inhibition by beta-mercaptoethanol (2.1 M) and L(+)-tartaric acid (20 mM). In addition, a second form of acid phosphatase that is tartrate resistant was found to be elevated in Gaucher serum. This form of serum acid phosphatase did not bind to Sulphopropyl Sephadex, was found to be significantly resistant to beta-mercaptoethanol (2.1 M), and was only partially inhibited by sodium dithionite (10 mM). The findings reported here indicate that at least three distinct forms of acid phosphatase activity are elevated in Gaucher's disease. Furthermore, the minor acid phosphatase activity contained in spleen homogenates has properties very similar to those of the major acid phosphatase activity observed to be present in serum of patients with Gaucher's disease. These data indicate that simple spleen spillage cannot account for the increased levels of serum acid phosphatase in patients with Gaucher's disease.
尽管所有戈谢病患者的主要基因缺陷都是葡糖脑苷脂酶活性缺乏，但脾脏和血清酸性磷酸酶活性显著升高的现象也几乎同样常见。戈谢病患者的脾脏和血清中至少含有两种酸性磷酸酶，通过在含有阳离子交换树脂磺丙基葡聚糖凝胶的柱上进行色谱分离，可以很容易地将它们分开。戈谢病患者脾脏的Triton X-100（1% v/v）提取物中所含的主要酸性磷酸酶（称为SP-I）占总活性的65%--95%，具有以下特性：（1）它不与阳离子交换柱结合；（2）其最适pH为4.5--5.0；（3）它被氟化钠（15 mM）、L(+)-酒石酸（20 mM）和β-巯基乙醇（2.1 M）抑制；（4）它对连二亚硫酸钠（10 mM）的抑制具有抗性。戈谢病患者脾脏提取物中存在的次要酸性磷酸酶活性（称为SP-II）具有与戈谢病患者血清中主要酸性磷酸酶活性相似的特性：（1）它与阳离子交换柱紧密结合（用0.5 M氯化钠洗脱）；（2）其最适pH为5.0--6.0；（3）它被氟化钠和连二亚硫酸钠抑制；（4）它对β-巯基乙醇（2.1 M）和L(+)-酒石酸（20 mM）的抑制具有抗性。此外，还发现戈谢病患者血清中一种抗酒石酸的酸性磷酸酶第二种形式升高。这种血清酸性磷酸酶形式不与磺丙基葡聚糖凝胶结合，对β-巯基乙醇（2.1 M）具有显著抗性，仅被连二亚硫酸钠（10 mM）部分抑制。此处报道的结果表明，戈谢病中至少有三种不同形式的酸性磷酸酶活性升高。此外，脾脏匀浆中所含的次要酸性磷酸酶活性与戈谢病患者血清中观察到的主要酸性磷酸酶活性特性非常相似。这些数据表明，单纯的脾脏渗漏不能解释戈谢病患者血清酸性磷酸酶水平的升高。
