P0515
Phospholipase D from Arachis hypogaea (peanut)
Type II, lyophilized powder, ≥60 units/mg protein
Synonyme(s) :
Lecithinase D, Phosphatidylcholine phosphatidohydrolase
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-639-8
MDL number:
Specific activity:
≥60 units/mg protein
Biological source:
Arachis hypogaea
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Laissez-nous vous aiderNom du produit
Phospholipase D from Arachis hypogaea (peanut), Type II, lyophilized powder, ≥60 units/mg protein
biological source
Arachis hypogaea
type
Type II
form
lyophilized powder
specific activity
≥60 units/mg protein
composition
Protein, ~30%
storage temp.
−20°C
Quality Level
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Analysis Note
Protein determined using biuret, unless otherwise indicated.
Application
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.
Biochem/physiol Actions
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.
General description
Phospholipase D is a phospholipid hydrolyzing enzyme and an important component of receptor-mediated signal transduction responses and regulated secretion.
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.
Other Notes
One unit will liberate 1.0 μmol of choline from L-α-phosphatidylcholine (egg yolk) per hr at pH 5.6 at 30 °C.
Physical form
Partially purified, lyophilized powder containing buffer salts
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Classe de stockage
11 - Combustible Solids
wgk
WGK 3
ppe
Eyeshields, Gloves, type N95 (US)
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Expression and characterization of rat brain phospholipase D
Xie Z, et al.
Methods in Enzymology, 345, 255-264 (2002)
Human neutrophil peptide receptors: mobilization mediated by phospholipase C.
Nelson R D, et al.
The American Journal of Pathology, 107(2), 202-202 (1982)
K D Philipson et al.
The Journal of biological chemistry, 259(1), 16-19 (1984-01-10)
Treatment of canine cardiac sarcolemmal vesicles with phospholipase D resulted in a large stimulation (up to 400%) of Na+-Ca2+ exchange activity. The phospholipase D treatment decreased the apparent Km (Ca2+) for the initial rate of Nai+-dependent Ca2+ uptake from 18.2
Sarah M Brejnholt et al.
Journal of the science of food and agriculture, 91(8), 1398-1405 (2011-03-10)
Phytases increase utilization of phytate phosphorus in feed. Since wheat is rich in endogenous phytase activity it was examined whether wheat phytases could improve phytate degradation compared to microbial phytases. Moreover, it was investigated whether enzymatic degradation of phytate is
Giuseppe Dionisio et al.
Plant physiology, 156(3), 1087-1100 (2011-01-12)
Barley (Hordeum vulgare) and wheat (Triticum aestivum) possess significant phytase activity in the mature grains. Maize (Zea mays) and rice (Oryza sativa) possess little or virtually no preformed phytase activity in the mature grain and depend fully on de novo
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