Muratova U Z, Bornikov V T, Abdukaiumova A Kh, Saatov T S
Biokhimiia. 1991 Feb;56(2):320-5.
The activity of phospholipase A2 in blood platelets of healthy donors and IHD patients was examined. The enzyme activity was found to be increased 3-fold in platelets possessing a high level of functional activity (IHD) and by one order of magnitude in patients with myocardial infarction as compared with healthy donors. An enzyme preparation possessing a phospholipase activity was isolated from platelets by using salt extraction (KCl) and sonication. Purification of the enzyme by affinity chromatography resulted in two protein peaks both having a phospholipase A2 activity, the purification and molecular masses of these fractions being 768- and 2200-fold, and 13.5 and 15 kDa, respectively. It was supposed that these proteins are substrate-specific forms of phospholipase A2.
对健康供体和缺血性心脏病（IHD）患者血小板中磷脂酶A2的活性进行了检测。结果发现，与健康供体相比，具有高水平功能活性（IHD）的血小板中酶活性增加了3倍，而心肌梗死患者的酶活性增加了一个数量级。通过盐提取（KCl）和超声处理从血小板中分离出具有磷脂酶活性的酶制剂。通过亲和色谱法对该酶进行纯化，得到两个均具有磷脂酶A2活性的蛋白峰，这些组分的纯化倍数和分子量分别为768倍和2200倍，以及13.5 kDa和15 kDa。推测这些蛋白质是磷脂酶A2的底物特异性形式。
