Principato G B, Bocchini V, Rosi G, Aisa M C, Giovannini E
Comp Biochem Physiol B. 1984;78(2):485-91. doi: 10.1016/0305-0491(84)90063-4.
Alkaline phosphatases (APs) present in Spirographis spallanzanii were extracted by water homogenization of butanol treatment. The enzymes solubilized as above were purified by acetone fractionation and then by DEAE-cellulose and Sephadex G-200 chromatography; separation of four AP forms was achieved, which were characterized by studying their molecular and catalytic properties. The various APs differ in molecular weight, electrophoretic mobility, optimum pH, but show similar Km values and substrate inhibition pattern. Kinetic studies carried out with several inhibitors show, in particular, the existence in these APs of a second binding site and suggest a possible role for them in the metabolism of phosphoric esters of the sugars.
通过丁醇处理后的水匀浆法提取了斯氏螺旋藻中存在的碱性磷酸酶（APs）。将上述溶解的酶依次通过丙酮分级分离、DEAE-纤维素和葡聚糖凝胶G-200色谱进行纯化；实现了四种AP形式的分离，并通过研究它们的分子和催化特性对其进行了表征。各种AP在分子量、电泳迁移率、最适pH方面存在差异，但显示出相似的Km值和底物抑制模式。特别是，用几种抑制剂进行的动力学研究表明，这些AP中存在第二个结合位点，并暗示它们在糖磷酸酯代谢中可能发挥作用。
