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P8398

Phospholipase D from cabbage

Type IV, lyophilized powder, ≥100 units/mg solid

Synonym(s):

Lecithinase D, Phosphatidylcholine phosphatidohydrolase, Phospholipase D from white cabbage

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Size/SKUAvailabilityPrice
500 units
Please contact Customer Service for Availability
5 760,00 CZK
2500 units
Please contact Customer Service for Availability
21 400,00 CZK

About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-639-8
MDL number:
EC Number:
Specific activity:
≥100 units/mg solid

5 760,00 CZK


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type

Type IV

Quality Segment

form

lyophilized powder

specific activity

≥100 units/mg solid

composition

Protein, ~25%

storage temp.

−20°C

General description

Phospholipase D (PLD) from cabbage comprises the C2 domain, PLD superfamily specific conserved regions (I–IV) with HxKx4Dx6GSxN (HKD) motif. Structurally, it is a barrel-shaped monomer bound to calcium ions.

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. Furthermore, PLD is used in purification and kinetic studies.
The enzyme has been used for the preparation of Bodipy-phosphatidylcholine during the preparation of fluorescently labelled lipids.

Biochem/physiol Actions

Phospholipase D from cabbage is widely used in biocatalytic transphosphatidylation reactions.
The amino acid sequence of cabbage PLD has 83% and 80% identity with Arabidopsis PLDα and castor bean PLD. It hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid.
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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This Item
P4912P0065P0515
description

Type IV, lyophilized powder, ≥100 units/mg solid

description

Type VII, lyophilized powder, ≥150 units/mg solid

description

≥50,000 units/mL, buffered aqueous glycerol solution

description

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

specific activity

≥100 units/mg solid

specific activity

≥150 units/mg solid

specific activity

≥50,000 units/mL

specific activity

≥60 units/mg protein

form

lyophilized powder

form

lyophilized powder

form

buffered aqueous glycerol solution

form

lyophilized powder

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−70°C

storage temp.

−20°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

type

Type IV

type

Type VII

type

-

type

Type II

composition

Protein, ~25%

composition

-

composition

-

composition

Protein, ~30%


Pictograms

Health hazard

Signal Word

Danger

Hazard Codes

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

WGK

WGK 3

PPE (personal protective equipment)

Eyeshields, Gloves, type N95 (US)



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Questions

1–2 of 2 Questions  
  1. How to measure the activity of PLD? Is there any specific buffer needed here? In my experiment, phosphatidylcholine cannot be hydrolyzed. Please give me a protocal to measure the activity of PLD.

    1 answer
    1. The activity of this product can be measured using a colorimetric assay that quantifies the liberation of choline from L-?-phosphatidylcholine as the substrate. The reaction buffer used is a sodium acetate buffer solution, pH 5.6 at 30°C. Detail of this assay protocol is available on the following web site: https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/320/272/p4912enz.pdf?srsltid=AfmBOopflybZ1u1LK4iLu-Wk3wGh2tCFmYL9TfZ8H45Ww4Mwb97rBZ08

      Helpful?

  2. How long will it remain stable after reconstitution at 4 degrees Celsius?

    1 answer
    1. 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).

      Helpful?

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