Identification and partial characterization of phospholipase D in the human amniotic membrane.
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).
Inamori
K
K
Department of Gynecology and Obstetrics, Kyoto University Faculty of Medicine, Japan.
Sagawa
N
N
Hasegawa
M
M
Itoh
H
H
Ueda
H
H
Kobayashi
F
F
Ihara
Y
Y
Mori
T
T
D000650:Amnion / Q000201:enzymology*; D002118:Calcium / Q000378:metabolism; D003902:Detergents; D000431:Ethanol / Q000494:pharmacology; D005230:Fatty Acids, Nonesterified / Q000378:metabolism; D005260:Female; D005865:Gestational Age; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism; D010739:Phospholipase D / Q000378:metabolism*; D011247:Pregnancy; D013347:Subcellular Fractions / Q000201:enzymology
D003902:Detergents; D005230:Fatty Acids, Nonesterified; D000431:Ethanol; D010739:Phospholipase D; D008274:Magnesium; D002118:Calcium