Related Experiment Video
Updated: Jul 10, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
[Properties of phospholipase D from rat liver mitochondria]
Abstract:
The properties of membrane-bound mitochondrial phospholipase D were investigated. The enzyme was shown to catalyze the hydrolysis of endogenous mitochondrial phospholipids, particularly phosphatidylethanolamine. The phospholipase activity was maximal at pH 5.0 and 7.0 was stimulated by Ca2+ and sodium oleate and was inhibited by SDS. The conditions for solubilization of the mitochondrial enzyme and its adsorption on a biospecific adsorbent were elaborated. The adsorption resulted in a 17-fold purification of the enzyme with a 33% yield. The adsorbed enzyme, similar to the membrane-bound one, was activated by Ca2+ and sodium oleate but, in contrast to the latter, was able to catalyze the hydrolysis of an exogenous substrate.
More Related Videos
08:49Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
Published on: March 14, 2021
10:31A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2
Published on: September 26, 2025
Related Concept Videos
Asymmetric Lipid Bilayer
Phosphoinositides and PIPs
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Overview of Fatty Acid Metabolism
Fatty acids are catabolized in a process called beta-oxidation, which takes place in the matrix of the mitochondria and converts their fatty acid chains into two-carbon units of acetyl groups. The acetyl...
Synthesis of Phosphatidylcholine in the ER Membrane
The major components of all eukaryotic cell...
IP3/DAG Signaling Pathway