Purification and Properties of a Phospholipase A2/Lipase Preferring Phosphatidic Acid, Bis(monoacylglycerol) Phosphate, and Monoacylglycerol from Rat Testis

• Published in: The Journal of biological chemistry Vol. 277; no. 46; pp. 43674 - 43681
• Main Authors: Ito, Masafumi, Tchoua, Urbain, Okamoto, Mitsuhiro, Tojo, Hiromasa
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 15.11.2002
• Subjects: Acyltransferases - metabolism; Animals; Catalysis; Chloroquine - pharmacology; Chromatography, High Pressure Liquid; Esterases - metabolism; Glycerides - chemistry; Glycerides - isolation & purification; Hydrogen-Ion Concentration; Hydrolysis; Lipid Metabolism; Liver - metabolism; Lysophospholipids - chemistry; Lysophospholipids - isolation & purification; Male; Mass Spectrometry; Monoglycerides; Pancreas - enzymology; Phospholipases A - metabolism; Phospholipases A2; Protein Structure, Tertiary; Rats; Rats, Sprague-Dawley; Substrate Specificity; Testis - enzymology; Testis - metabolism

Phospholipase A 2 (PLA 2 ) was purified to homogeneity from the supernatant fraction of rat testis homogenate. The purified 63-kDa enzyme did not require Ca 2+ ions for activity and exhibited both phosphatidic acid-preferring PLA 2 and monoacylglycerol lipase activities with a modest specificity tow...