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Safety Information

P0515

Sigma-Aldrich

Phospholipase D from Arachis hypogaea (peanut)

Type II, lyophilized powder, ≥60 units/mg protein

Synonym(s):

Lecithinase D, Phosphatidylcholine phosphatidohydrolase

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About This Item

CAS Number:
9001-87-0
Enzyme Commission number:
3.1.4.4 (BRENDA, IUBMB)
EC Number:
232-639-8
MDL number:
MFCD00131897
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Arachis hypogaea

Quality Level

200

type

Type II

form

lyophilized powder

specific activity

≥60 units/mg protein

composition

Protein, ~30%

storage temp.

−20°C

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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.

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.

Unit Definition

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

Analysis Note

Protein determined using biuret, unless otherwise indicated.

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

P0515-10KU:
P0515-VAR:
P0515-2.5KU-PW:
P0515-2.5KU:
P0515-1KU:
P0515-BULK:
P0515-25KU:

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Certificates of Analysis (COA)

Lot/Batch Number
11190167
069M4141V
068M4034V
11171125
117M4149V

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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
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)
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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