Brocklehurst D, Lathe G H, Aparicio S R
Clin Chim Acta. 1976 Mar 15;67(3):269-79. doi: 10.1016/0009-8981(76)90335-1.
The nature of the stationary band of alkaline phosphatase, which occurs on starch gel electrophoresis of sera from patients with biliary obstruction, has been examined. Stationary alkaline phosphatase was eluted from Sepharose 4-B gel close to the void volume and together with the plasma membrane enzymes, nucleotide pyrophosphatase and 5'-nucleotidase, and with lipoprotein-X. Electron microscopy of concentrates of stationary alkaline phosphatase, prepared by ultracentrifugation and gel filtration, showed large (0.3--1 mum diameter) and small structures (30-70 nm diameter) by negative staining. The activity of the stationary alkaline phosphatase was associated in fixed sections with particles of about 10 nm X 40 nm resembling those of lipoprotein-X. It is suggested that the stationary alkaline phosphatase does not move into starch gel during electrophoresis because it is particulate. In agar electrophoresis the alkaline phosphatase which was stationary on starch gel moved towards the cathode with lipoprotein-X.
对胆道梗阻患者血清在淀粉凝胶电泳上出现的碱性磷酸酶固定带的性质进行了研究。固定性碱性磷酸酶从琼脂糖4 - B凝胶上接近空体积处洗脱下来，与质膜酶、核苷酸焦磷酸酶和5'-核苷酸酶以及脂蛋白-X一起洗脱。通过超速离心和凝胶过滤制备的固定性碱性磷酸酶浓缩物的电子显微镜检查显示，经负染色后有大的结构（直径0.3 - 1μm）和小的结构（直径30 - 70nm）。在固定切片中，固定性碱性磷酸酶的活性与约10nm×40nm的颗粒相关，类似于脂蛋白-X的颗粒。有人提出，固定性碱性磷酸酶在电泳过程中不进入淀粉凝胶是因为它是颗粒状的。在琼脂电泳中，在淀粉凝胶上固定的碱性磷酸酶与脂蛋白-X一起向阴极移动。
