Inamori K, Sagawa N, Hasegawa M, Itoh H, Ueda H, Kobayashi F, Ihara Y, Mori T
Department of Gynecology and Obstetrics, Kyoto University Faculty of Medicine, Japan.
Biochem Biophys Res Commun. 1993 Mar 31;191(3):1270-7. doi: 10.1006/bbrc.1993.1354.
The enzymatic activity of phospholipase D and its characteristics have been examined in human amnion tissue. The phospholipase D activity was not Ca(2+)- or Mg(2+)-dependent and was activated by unsaturated fatty acids. The optimal pH of phospholipase D was 5.5. The phospholipase D activity in amnion tissue was highest in the microsomal fraction, and preferentially utilized phosphatidylcholine as a substrate. The phospholipase D activity of the microsomal fraction of amnion tissue obtained at term before labor onset (34.0 +/- 16.3 nmol/hour/mg protein, mean +/- SD, n = 11) was significantly (p < 0.05) higher than the activity in this tissue obtained from women in the mid-trimester (15.0 +/- 7.5 nmol/hour/mg protein, n = 9).
已对人羊膜组织中磷脂酶D的酶活性及其特性进行了检测。磷脂酶D的活性不依赖于Ca(2+)或Mg(2+)，并被不饱和脂肪酸激活。磷脂酶D的最适pH为5.5。羊膜组织中的磷脂酶D活性在微粒体部分最高，且优先利用磷脂酰胆碱作为底物。足月临产前获得的羊膜组织微粒体部分的磷脂酶D活性（34.0±16.3 nmol/小时/毫克蛋白，平均值±标准差，n = 11）显著高于（p < 0.05）孕中期妇女该组织中的活性（15.0±7.5 nmol/小时/毫克蛋白，n = 9）。
