Merck, P9279-1MG, Phospholipase A2 from honey bee venom (Apis mellifera)

General description
Phospholipase A2 from honey bee venom (Apis mellifera) is a calcium-dependent lipolytic enzyme.
Application
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

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.
Analysis Note
Protein determined by biuret.
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 8.9 at 25 °C.