Phospholipase D (PLD) is abundantly found in the eukaryotes and prokaryotes. It is present in all mammalian cells. In mammals, PLD is initiated by various hormones, neurotransmitters, growth factors and cytokines.
Phospholipase D is a phospholipid hydrolyzing enzyme and an important component of receptor-mediated signal transduction responses and regulated secretion.
Phospholipase D from Arachis hypogaea (peanut) has been used in the preparation of lipase enzyme solution. It has also been used to determine its influence on human neutrophil respiratory function.
Research has shown ADP-ribosylation factor regulation of phospholipase D is important in the release of nascent secretory vesicles from the trans-Golgi network. It has also been used in a study to investigate stimulation of Na+-Ca2+ exchange activity in canine cardiac sarcolemmal vesicals.
Hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid.
Phospholipase D is involved in conferring drought susceptibility in peanuts, which increases the risk of aflatoxin contamination.
Phospholipase D (PLD) modulates cell growth, secretion and the actin cytoskeleton.
One unit will liberate 1.0 μmol of choline from L-α-phosphatidylcholine (egg yolk) per hr at pH 5.6 at 30 °C.
Partially purified, lyophilized powder containing buffer salts
Protein determined using biuret, unless otherwise indicated.