Etienne J, Gruber A, Polonovski J
Biochimie. 1982 May;64(5):377-80. doi: 10.1016/s0300-9084(82)80443-4.
Rat blood platelet lysate showed high phospholipase A2 activity and contained much less than activating factor much greater than which increased phospholipase A2 activity. The phospholipase A2 and the much less than activating factor much greater than were eluted together in the same first protein fraction obtained by chromatography on a G 100 Sephadex column washed with tris-HCl buffer (pH 7.2). This mixture of proteins can be further fractionated on a Sepharose Blue CL 6B column in 2 protein fractions. The first fraction eluted by tris-HCl buffer (pH 7.2) showed 10 percent of the initial phospholipase activity; the second fraction eluted by NaCl 1 M-tris HCl buffer (pH 7.2) which showed no phospholipase activity, contains activating factor; if both fractions are mixed the initial phospholipase activity is almost totally restored. In conclusion, in rat blood platelets, phospholipase activity originates in a great part from the association of an much less than activable phospholipase much greater than and an much less than activating factor much greater than.
大鼠血小板裂解液显示出高磷脂酶A2活性，且所含的激活因子远少于能增加磷脂酶A2活性的物质。磷脂酶A2和该激活因子在经三羟甲基氨基甲烷 - 盐酸缓冲液（pH 7.2）洗脱的G 100葡聚糖凝胶柱层析得到的同一首个蛋白组分中一起被洗脱下来。这种蛋白质混合物可在琼脂糖蓝CL 6B柱上进一步分离成两个蛋白组分。用三羟甲基氨基甲烷 - 盐酸缓冲液（pH 7.2）洗脱的首个组分显示出初始磷脂酶活性的10%；用1M氯化钠 - 三羟甲基氨基甲烷盐酸缓冲液（pH 7.2）洗脱的第二个组分虽无磷脂酶活性，但含有激活因子；若将这两个组分混合，初始磷脂酶活性几乎能完全恢复。总之，在大鼠血小板中，磷脂酶活性很大程度上源于一种难以激活的磷脂酶与一种激活因子的结合。
