P6534
Phospholipase A2 from porcine pancreas
ammonium sulfate suspension, ≥600 units/mg protein
Synonyme(s) :
Lecithinase A, PLA2, Phosphatidylcholine 2-acylhydrolase
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A propos de cet article
Numéro CAS:
UNSPSC Code:
12352204
NACRES:
NA.32
EC Number:
232-637-7
MDL number:
Specific activity:
≥600 units/mg protein
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Laissez-nous vous aiderNom du produit
Phospholipase A2 from porcine pancreas, ammonium sulfate suspension, ≥600 units/mg protein
form
ammonium sulfate suspension
specific activity
≥600 units/mg protein
UniProt accession no.
storage temp.
2-8°C
Quality Level
Gene Information
pig ... PLA2G1B(445525)
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Analysis Note
Protein determined by biuret.
Application
Phospholipase A2 has been used in phospholipase assay and to determine rat renal proximal tubular segments (PTS) viability during oxygenation and hypoxia-reoxygenation.
Biochem/physiol Actions
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.
It has a high catalytic activity on aggregated substrates compared to monomeric substrates.
General description
Phospholipase A2 is a small disulfide-rich protein having 124 residues. It is a calcium-dependent enzyme.
Other Notes
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.
Physical form
Suspension in 3.2 M (NH4)2SO4 solution, pH 5.5
Classe de stockage
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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A A Grippo et al.
Journal of reproduction and fertility, 102(1), 87-93 (1994-09-01)
Cholesterol and phospholipid concentrations and phospholipase activity were measured in fluid from cannulae collected from the bovine oviductal isthmus and ampulla at different stages of the oestrous cycle. The cholesterol concentration and cholesterol normalized by protein were significantly (P =
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
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
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