Phospholipase A2 from honey bee venom (Apis mellifera) is a calcium-dependent lipolytic enzyme.
Phospholipase A2 from honey bee venom (Apis mellifera) has been used
- to determine renal proximal tubular segments (PTS) viability during oxygenation and hypoxia-reoxygenation
- in the treatment of photosystem-II (PSII) dimer complex of Synechocystis to study changes in oxygen-evolving activity
- as a standard in phospholipase activity assay
1, 5, 25 mg in glass bottle
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.
One unit will hydrolyze 1.0 μmole of soybean L-α-phosphatidylcholine to L-α-lysophosphatidylcholine and a fatty acid per min at pH 8.9 at 25 °C.
Protein determined by biuret.