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Related Experiment Videos

Membrane-associated phospholipase D activity in rat sciatic nerve.

J Chattopadhyay1, V Natarajan, H H Schmid

  • 1Hormel Institute, University of Minnesota, Austin 55912.

Journal of Neurochemistry
|October 1, 1991
PubMed
Summary
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Rat sciatic nerve contains a membrane-bound phospholipase D enzyme that breaks down phosphatidylcholine (PC) into phosphatidic acid (PA) and choline. This enzyme also shows transphosphatidylation activity with ethanol, producing phosphatidylethanol.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Enzymology

Background:

  • The rat sciatic nerve possesses a membrane-bound phospholipase D enzyme.
  • This enzyme is primarily located in the microsomal and myelin fractions.
  • Associated phosphatidate phosphohydrolase activity produces diacylglycerols (DAG).

Purpose of the Study:

  • To characterize the activity and properties of phospholipase D in the rat sciatic nerve.
  • To investigate the enzyme's substrate specificity and reaction products.
  • To explore the enzyme's transphosphatidylation capabilities.

Main Methods:

  • Enzyme assays using exogenous phosphatidylcholine (PC) as a substrate.
  • Analysis of reaction products including phosphatidic acid (PA), diacylglycerols (DAG), and phosphatidylethanol.

Related Experiment Videos

  • Investigation of enzyme kinetics, pH optimum, and inhibition by NaF.
  • Assessment of transphosphatidylation activity in the presence of varying ethanol concentrations.

    • Main Results:

    • Phospholipase D activity requires detergent, with an optimum pH of 6.5.
    • NaF inhibits phosphatidate phosphohydrolase activity.
    • The enzyme exhibits transphosphatidylation activity, forming phosphatidylethanol in the presence of ethanol.
    • Optimal conditions yield PC hydrolysis at 15 nmol/h/mg protein.

    Conclusions:

    • Rat sciatic nerve contains a functional phospholipase D with associated enzymes.
    • The enzyme's activity is modulated by factors like pH, detergent, and NaF.
    • The demonstrated transphosphatidylation activity suggests potential roles in lipid metabolism and signaling pathways.