P0515
Phospholipase D from Arachis hypogaea (peanut)
Type II, lyophilized powder, ≥60 units/mg protein
Synonym(s):
Lecithinase D, Phosphatidylcholine phosphatidohydrolase
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biological source
Arachis hypogaea
Quality Level
type
Type II
form
lyophilized powder
specific activity
≥60 units/mg protein
composition
Protein, ~30%
storage temp.
−20°C
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This Item | P4912 | P8913 | L7381 |
|---|---|---|---|
| specific activity ≥60 units/mg protein | specific activity ≥150 units/mg solid | specific activity ≥20 units/mg protein | specific activity - |
| biological source Arachis hypogaea | biological source Streptomyces sp. | biological source - | biological source - |
| form lyophilized powder | form lyophilized powder | form lyophilized powder | form lyophilized powder |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
| type Type II | type Type VII | type - | type - |
General description
Phospholipase D is a phospholipid hydrolyzing enzyme and an important component of receptor-mediated signal transduction responses and regulated secretion. [1]
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.[2]
Application
Phospholipase D from Arachis hypogaea (peanut) has been used in the preparation of lipase enzyme solution.[3] It has also been used to determine its influence on human neutrophil respiratory function.[4]
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. [5]
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. [6]
Phospholipase D (PLD) modulates cell growth, secretion and the actin cytoskeleton.[2]
Physical form
Partially purified, lyophilized powder containing buffer salts
Analysis Note
Protein determined using biuret, unless otherwise indicated.
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.
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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
Human neutrophil peptide receptors: mobilization mediated by phospholipase C.
Nelson R D, et al.
The American Journal of Pathology, 107(2), 202-202 (1982)
Expression and characterization of rat brain phospholipase D
Xie Z, et al.
Methods in Enzymology, 345, 255-264 (2002)
B Z Guo et al.
Planta, 223(3), 512-520 (2005-10-04)
Preharvest aflatoxin contamination has been identified by the peanut industry as a serious issue in food safety and human health because of the carcinogenic toxicity. Drought stress is the most important environmental factor exacerbating Aspergillus infection and aflatoxin contamination in
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
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