P4912
Phospholipase D from Streptomyces sp.
Type VII, lyophilized powder, ≥150 units/mg solid
Synonym(s):
Lecithinase D, Phosphatidylcholine phosphatidohydrolase
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About This Item
biological source
Streptomyces sp.
Quality Level
type
Type VII
form
lyophilized powder
specific activity
≥150 units/mg solid
storage temp.
−20°C
Application
Phospholipase D (PLD) has been used to hydrolyze the phosphate bonds of phospholipids and sphingomyelin to yield 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 has been used in purification and kinetic studies.
The enzyme from Sigma has been used in the translocation of sphingosine kinase 1 (SK1) to membrane fractions under in vitro conditions. It has also been used to produce phosphatidic acid (PA) from phosphatidylcholine (PC) in HL60 permeabilized cells.
Biochem/physiol Actions
Phospholipase D is glycerophospholipid-specific. It is markedly less active on sphingomyelins and lysophospholipids. Phospholipase D 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.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Unit Definition
One unit will liberate 1.0 μmole of choline from 1,2-Dioleoyl-sn-glycero-3-phosphocholine per hour at pH 8.0 at 37 °C.
Analysis Note
Protein by biuret
inhibitor
Product No.
Description
Pricing
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
WGK
WGK 3
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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The Journal of biological chemistry, 279(43), 44763-44774 (2004-08-18)
Sphingosine kinase 1 (SK1) phosphorylates sphingosine to generate sphingosine 1-phosphate (S1P). Because both substrate and product of the enzyme are potentially important signaling molecules, the regulation of SK1 is of considerable interest. We report that SK1, which is ordinarily a
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