Bonnefis M J, Rey G, Thouvenot J P, Douste-Blazy L
Biochimie. 1977;59(4):355-61. doi: 10.1016/s0300-9084(77)80311-8.
Phospholipase activities of rat intestinal mucosa homogenate have been determined from lysophosphatidylcholines [14C] and phosphatidylcholines [-3H-14C]. In the presence of phosphatidylcholines, at pH 6.5, the homogenate has a phospholipase B activity. At pH 8.5, a phospholipase A2 activity was shown. In the presence of lysophospatidylcholines, at pH 6.5, we notice a lysophospholipase A1 activity. A kinetic study of the reactions allows us to separate the activity B into a phospholipase A2 activity and a lysophospholipase A1 activity. Thus, it appears that the total phospholipase activity of rat intestinal mucosa would results from a phospholipase A2 activity and a lysophospholipase A1 activity.
已使用溶血磷脂酰胆碱[14C]和磷脂酰胆碱[-3H-14C]测定了大鼠肠黏膜匀浆的磷脂酶活性。在磷脂酰胆碱存在的情况下,pH为6.5时,匀浆具有磷脂酶B活性。在pH 8.5时,显示出磷脂酶A2活性。在溶血磷脂酰胆碱存在的情况下,pH为6.5时,我们注意到有溶血磷脂酶A1活性。对这些反应的动力学研究使我们能够将B活性分离为磷脂酶A2活性和溶血磷脂酶A1活性。因此,似乎大鼠肠黏膜的总磷脂酶活性是由磷脂酶A2活性和溶血磷脂酶A1活性产生的。