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MilliporeSigma

P8804

Sigma-Aldrich

Phospholipase C, Phosphatidylinositol-specific from Bacillus cereus

buffered aqueous glycerol solution, ≥1,000 units/mg protein (Lowry)

Synonym(s):

1-Phosphatidyl-D-myo-inositol inositol phosphohydrolase, cyclic-phosphate forming, PI-PLC

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About This Item

CAS Number:
37288-19-0
EC Number:
4.6.1.13 (BRENDA, IUBMB)
EC Number:
232-638-2
MDL number:
MFCD00131896
UNSPSC Code:
12352204
NACRES:
NA.32

Key Documents

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biological source

Bacillus sp. (Bacillus cereus)

Quality Level

200

form

buffered aqueous glycerol solution

specific activity

≥1,000 units/mg protein (Lowry)

mol wt

28 kDa

foreign activity

Phopholipase C (lecithinase) ≤1 units/mg protein
Sphingomyelinase ≤40 units/mg protein

storage temp.

2-8°C

Gene Information

Bacillus cereus E33L ... BCZK3513(3026815)

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General description

Phospholipase C (PI-PLC) from Bacillus cereus has irregular triosephosphate isomerase (TIM)-barrel structure with eight-standard parallel β barrel. It is a 28 kDa protein.

Application

Phospholipase C, Phosphatidylinositol-specific from Bacillus cereus has been used:
  • in the hydrolysis of substrates p-nitrophenylphosphorylcholine (p-NPPC) and p-nitrophenylphosphorylphosphate (p-NPP)
  • to cleave glycosylphosphatidylinositol (GPI) anchor of lynx1 protein and its detachment from plasma membrane
  • to cleave immunolabeled HeLa cells

Biochem/physiol Actions

Phospholipase C (PI-PLC) releases diacylglycerol by cleaving the glycosylphosphatidylinositol. It has broad substrate specificity and its activity is influenced by metal ions and surfactants.
Used for the release of GPI anchored proteins from the membrane.

Physical form

Solution in 60% (v/v) glycerol containing 10 mM Tris-HCl, pH 8.0 and 10 mM EDTA

Analysis Note

Acetylcholinesterase is measured according to Ellman, et al.

Other Notes

One unit will liberate one unit of acetylcholinesterase per minute from a membrane-bound crude preparation at pH 7.4 at 30 °C (10 minute incubation).

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
029M4097V
11181012
088M4118V
067M4192V
124M4051V

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Ligand binding characteristics of a glycosylphosphatidyl inositol membrane-anchored HeLa cell folate receptor epitope-related to human milk folate binding protein
Holm J, et al.
Bioscience Reports, 20(2), 109-118 (2000)
Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl (alpha1? 6)-d-myo-inositol, an essential fragment of GPI anchors
Heinz DW, et al.
Biochemistry, 35(29), 9496-9504 (1996)
Critical evaluation of p-nitrophenylphosphorylcholine (p-NPPC) as artificial substrate for the detection of phospholipase C
Flieger A, et al.
Enzyme and Microbial Technology, 26(5-6), 451-458 (2000)
Lynx1 shifts alpha4beta2 nicotinic receptor subunit stoichiometry by affecting assembly in the endoplasmic reticulum
Nichols WA, et al.
The Journal of Biological Chemistry, 289(45), 31423-31432 (2014)
M G Low et al.
The Biochemical journal, 167(1), 281-284 (1977-10-01)
Purified phosphatidylinositol-specific phospholipase C from Staphylococcus aureus released a substantial proportion of the total alkaline phosphatase activity from a wide range of tissues from several mammalian species. Co-purification of the phospholipase C and alkaline phosphatase-releasing activities and the inhibition of
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Articles

Glycosylphosphatidylinisotol-anchored Glycoproteins Overview

Glycosylphosphatidylinisotol- (GPI) anchored proteins have been identified throughout a broad range of eukaryotic species ranging from humans to insects, yeasts, bacteria, and fungi, suggesting that they are an ancient modification.

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