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P6534

Sigma-Aldrich

Phospholipase A2 from porcine pancreas

ammonium sulfate suspension, ≥600 units/mg protein

Synonyme(s) :

Lecithinase A, PLA2, Phosphatidylcholine 2-acylhydrolase

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About This Item

Numéro CAS:
9001-84-7
Numéro de classification (Commission des enzymes):
3.1.1.4 (BRENDA, IUBMB)
Numéro CE :
232-637-7
Numéro MDL:
MFCD00131890
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32

Forme

ammonium sulfate suspension

Activité spécifique

≥600 units/mg protein

Numéro d'accès UniProt

P00592

Température de stockage

2-8°C

Informations sur le gène

pig ... PLA2G1B(445525)

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Description générale

Phospholipase A2 is a small disulfide-rich protein having 124 residues. It is a calcium-dependent enzyme.

Application

Phospholipase A2 has been used in phospholipase assay and to determine rat renal proximal tubular segments (PTS) viability during oxygenation and hypoxia-reoxygenation.

Actions biochimiques/physiologiques

It has a high catalytic activity on aggregated substrates compared to monomeric substrates.
Hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Preferred substrates are phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogues. Phosphatidylinositol and phosphatidylserine are also hydrolyzed. Aggressively attacks phospholipids in membranes of intact cells.

Définition de l'unité

One unit will hydrolyze 1.0 μmole of soybean L-α-phosphatidylcholine to L-α-lysophosphatidylcholine and a fatty acid per min at pH 8.0 at 37 °C.

Forme physique

Suspension in 3.2 M (NH4)2SO4 solution, pH 5.5

Remarque sur l'analyse

Protein determined by biuret.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Sigma-Aldrich

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B van den Berg et al.
The EMBO journal, 14(17), 4123-4131 (1995-09-01)
The lipolytic enzyme phospholipase A2 (PLA2) is involved in the degradation of high-molecular weight phospholipid aggregates in vivo. The enzyme has very high catalytic activities on aggregated substrates compared with monomeric substrates, a phenomenon called interfacial activation. Crystal structures of
Knut Kölbel et al.
Biophysical chemistry, 206, 12-21 (2015-06-29)
Porcine pancreatic phospholipase A2, a small and disulfide rich protein, is extremely resistant against chemically or thermally induced unfolding. Despite this marked resistance, the protein displays broad unfolding transitions resulting in comparatively low apparent thermodynamic stability. Broad unfolding transitions may
R A Zager et al.
Proceedings of the National Academy of Sciences of the United States of America, 90(17), 8297-8301 (1993-09-01)
During hypoxic or ischemic renal tubular injury, phospholipase A2 (PLA2) induces membrane deacylation, causing fatty acid accumulation and phospholipid breakdown. Because these changes can compromise cellular integrity, PLA2 activity has been widely proposed as a critical mediator of hypoxic renal
Elena Venuti et al.
Journal of cystic fibrosis : official journal of the European Cystic Fibrosis Society, 16(6), 763-770 (2017-07-26)
Bile salt stimulated lipase (BSSL; Enzyme Commission (EC) number 3.1.1.13) has been a candidate triglyceridase for improving enzyme therapy for pancreatic insufficiency; however, its efficacy is near absent. We hypothesise that similarly to pancreatic lipase, BSSL is inhibited by phospholipids
B van den Berg et al.
Journal of biomolecular NMR, 5(2), 110-121 (1995-02-01)
The three-dimensional structure of porcine pancreatic PLA2 (PLA2), present in a 40 kDa ternary complex with micelles and a competitive inhibitor, has been determined using multidimensional heteronuclear NMR spectroscopy. The structure of the protein (124 residues) is based on 1854
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How to Work with Enzymes Supplied as Ammonium Sulfate Suspensions

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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