Thuren T, Eklund K K, Virtanen J A, Kinnunen P K
Department of Medical Chemistry, University of Helsinki, Finland.
Chem Phys Lipids. 1990 Jul;55(1):55-60. doi: 10.1016/0009-3084(90)90149-l.
Hydrolysis by pancreatic and snake venom (Crotalus atrox) phospholipase A2 of fluorescent monolayers of pyrene-labelled phosphatidylglycerol on solid support was studied. We used a fluorescence microscope equipped with video camera, video recorder and an image analyzer to monitor changes in fluorescence. Decrease in pyrene excimer emission was evident when pyrene phosphatidylglycerol monolayers transferred onto quartz glass slides (at a surface pressure of 15 mN m-1) were subjected to enzymatic hydrolysis. Snake venom phospholipase A2 could hydrolyze the monolayers almost completely while pancreatic phospholipase A2 could cause only 50% decrease in fluorescence intensity. EDTA totally inhibited the action of both A2 phospholipases. When monolayers were transferred onto solid supports at a surface pressure of 31 mN m-1 C. atrox phospholipase A2 could still exert activity whereas porcine pancreatic phospholipase A2 was inactive.
研究了在固体支持物上芘标记的磷脂酰甘油荧光单层被胰腺和蛇毒（锯鳞蝰）磷脂酶A2水解的情况。我们使用配备了摄像机、录像机和图像分析仪的荧光显微镜来监测荧光变化。当转移到石英载玻片上（表面压力为15 mN m-1）的芘磷脂酰甘油单层受到酶水解时，芘激基复合物发射明显减少。蛇毒磷脂酶A2几乎可以完全水解单层，而胰腺磷脂酶A2只会使荧光强度降低50%。EDTA完全抑制了两种A2磷脂酶的作用。当单层在31 mN m-1的表面压力下转移到固体支持物上时，锯鳞蝰磷脂酶A2仍能发挥活性，而猪胰腺磷脂酶A2则无活性。
