Identification and partial characterization of phospholipase D in the human amniotic membrane

Biochem Biophys Res Commun. 1993 Mar 31;191(3):1270-7. doi: 10.1006/bbrc.1993.1354.

Abstract

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).

MeSH terms

  • Amnion / enzymology*
  • Calcium / metabolism
  • Detergents
  • Ethanol / pharmacology
  • Fatty Acids, Nonesterified / metabolism
  • Female
  • Gestational Age
  • Humans
  • Hydrogen-Ion Concentration
  • Kinetics
  • Magnesium / metabolism
  • Phospholipase D / metabolism*
  • Pregnancy
  • Subcellular Fractions / enzymology

Substances

  • Detergents
  • Fatty Acids, Nonesterified
  • Ethanol
  • Phospholipase D
  • Magnesium
  • Calcium