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P7633

Sigma-Aldrich

Phospholipase C from Clostridium perfringens (C. welchii)

greener alternative

Type I, lyophilized powder, 10-50 units/mg protein

Synonym(s):

Lecithinase C, Lipophosphodiesterase I, PC-PLC, Phosphatidylcholine cholinephosphohydrolase

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About This Item

CAS Number:
9001-86-9
Enzyme Commission number:
3.1.4.3 (BRENDA, IUBMB)
EC Number:
232-638-2
MDL number:
MFCD00131895
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bacterial (Clostridium perfringens)

Quality Level

200

type

Type I

form

lyophilized powder

specific activity

10-50 units/mg protein

composition

protein, 20-40%

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

sustainability

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application(s)

diagnostic assay manufacturing

greener alternative category

, Enabling

storage temp.

−20°C

Gene Information

Clostridium perfringens str. 13 ... plc(988262)

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General description

We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in biodiesel research. For more information see the article in biofiles.

Application

Phospholipase C (PLC) has been used to study adrenoceptor-mediated transmembrane signaling. It is also used to degrade inositol-containing phospholipids. Furthermore, it has been used to study 9E3 gene activation.

Biochem/physiol Actions

PLC hydrolyzes the phosphate bond on phosphatidylcholine and other glycerophospholipids yielding diacylglycerol. This enzyme also hydrolyzes the phosphate bonds of sphingomyelin, cardiolipin, choline plasmalogen and ceramide phospholipids. Phospholipase C is induced by thrombin and platelet-activating factor, forming 1,2-diacylglycerol and phosphatidic acid.
Hydrolyzes the phosphate bond on phosphatidylcholine and other glycerophospholipids yielding diacylglycerol; this enzyme will also hydrolyze the phosphate bonds of sphingomyelin, cardiolipin, choline plasmalogen and ceramide phospholipids.

Unit Definition

One unit will liberate 1.0 μmole of water soluble organic phosphorus from egg yolk L-α-phosphatidylcholine per min at pH 7.3 at 37 °C.

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

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)

Certificates of Analysis (COA)

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Mojtaba Alimolaei et al.
Probiotics and antimicrobial proteins, 10(2), 251-257 (2017-04-13)
The alpha-toxin is one of the virulence factors of Clostridium perfringens for gas gangrene in humans and animals or necrotic enteritis in poultry. The C-terminal domain of this toxin ( cpa 247-370 ) was synthesized and cloned into pT1NX vector
R Spangler et al.
Proceedings of the National Academy of Sciences of the United States of America, 86(18), 7017-7021 (1989-09-01)
Induction of the transformation-related gene 9E3 by the v-src and v-fps gene products (v-Src and v-Fps) is blocked in chicken embryo fibroblasts depleted of protein kinase C (PKC). PKC agonists induce 9E3 gene expression. Protein kinase inhibitors block v-Src- and
N Sieger et al.
Arthritis and rheumatism, 65(3), 770-779 (2012-12-13)
CD22 is a surface molecule exclusively expressed on B cells that regulates adhesion and B cell receptor (BCR) signaling as an inhibitory coreceptor of the BCR. Central downstream signaling molecules that are activated upon BCR engagement include spleen tyrosine kinase
Purification of Clostridium perfringens phospholipase C (alpha-toxin) by affinity chromatography on agarose-linked egg-yolk lipoprotein.
T Takahashi et al.
Biochimica et biophysica acta, 351(1), 155-171 (1974-05-10)
Zhou Zhou et al.
Circulation, 127(4), 476-485 (2012-12-26)
Platelet hyperactivity induced by inflammation is a known risk factor for atherosclerosis and thrombosis, but its underlying mechanisms remain poorly understood. The signal transducer and activator of transcription 3 (STAT3) was activated in collagen-stimulated platelets. Activated STAT3 served as a
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