Upon the addition of crystalline serum albumin (10 mg/mL) and storage at -15°C, solutions of this product in water are stable for several months. Additional information can be found in the Methods in Enzymology XIV, 202 (1969).
P8398
Phospholipase D from cabbage
Type IV, lyophilized powder, ≥100 units/mg solid
Synonim(y):
Lecithinase D, Phosphatidylcholine phosphatidohydrolase, Phospholipase D from white cabbage
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500 UNITS
963,00 zł
2500 UNITS
3500,00 zł
963,00 zł
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Informacje o tej pozycji
Numer CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-639-8
MDL number:
Specific activity:
≥100 units/mg solid
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Type IV
form
lyophilized powder
specific activity
≥100 units/mg solid
composition
Protein, ~25%
storage temp.
−20°C
Quality Level
1 of 4
Ta pozycja | |||
|---|---|---|---|
| specific activity ≥100 units/mg solid | specific activity ≥150 units/mg solid | specific activity ≥1,000 units/mg protein (Lowry) | specific activity 10-50 units/mg protein |
| 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 300 | Quality Level 200 |
| type Type IV | type Type VII | type - | type Type I |
| composition Protein, ~25% | composition - | composition - | composition protein, 20-40% |
General description
Application
Phospholipase D (PLD) is used to hydrolyze the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid. It has also been used to study metabolic labeling and direct imaging of choline phospholipids in vivo by measuring propargyl-Cho incorporation[2]. Furthermore, PLD is used in purification and kinetic studies[3].
The enzyme has been used for the preparation of Bodipy-phosphatidylcholine during the preparation of fluorescently labelled lipids.[4]
Biochem/physiol Actions
Hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid.
Phospholipase D from cabbage is widely used in biocatalytic transphosphatidylation reactions.[5]
The amino acid sequence of cabbage PLD has 83% and 80% identity with Arabidopsis PLDα and castor bean PLD[6]. It hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid.
Analysis Note
Protein determined using biuret.
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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related product
Numer produktu
Opis
Cennik
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Klasa składowania
11 - Combustible Solids
wgk
WGK 3
ppe
Eyeshields, Gloves, type N95 (US)
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
Susanne Stumpe et al.
The FEBS journal, 274(10), 2630-2640 (2007-04-25)
Phospholipases D play an important role in the regulation of cellular processes in plants and mammals. Moreover, they are an essential tool in the synthesis of phospholipids and phospholipid analogs. Knowledge of phospholipase D structures, however, is widely restricted to
Premysl Pejchar et al.
The New phytologist, 188(1), 150-160 (2010-07-16)
• Aluminium ions (Al) have been recognized as a major toxic factor for crop production in acidic soils. This study aimed to assess the impact of Al on the activity of phosphatidylcholine-hydrolysing phospholipase C (PC-PLC), a new member of the
PLD3 is a neuronal lysosomal phospholipase D associated with I?-amyloid plaques and cognitive function in Alzheimer's disease.
Nackenoff, et al.
PLoS Genetics, 17, e1009406-e1009406 (2021)
T T Allgyer et al.
Biochemistry, 18(24), 5348-5353 (1979-11-27)
Phospholipase D has been purified 680-fold from an acetone powder of savoy cabbage in an overall yield of 30%. The purification involves solubilization of the acetone powder in a Ca2+-containing buffer and subsequent ammonium sulfate fractionation. Gel filtration on Sephadex
Alexandra Lerchner et al.
Protein engineering, design & selection : PEDS, 19(10), 443-452 (2006-07-18)
In addition to hydrolysis of glycerophospholipids, phospholipases D (PLDs) catalyze the head group exchange. The molecular basis of this transphosphatidylation potential, which strongly varies for PLDs from different sources, is unknown hitherto. Recently, the genes of two PLD isoenzymes from
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