title: Purification and characterization of phospholipase A2 from bovine prostate.
abstract: Phospholipase A2 (PLA2) was purified from bovine prostate by ammonium sulphate precipitation and fractionation by anion exchange chromatography, chromatofocusing and gel filtration. The purified enzyme was Ca(2+)-dependent and had a pH-optimum of 8.0. Ba2+, Fe2+, Hg2+, Mg2+, Pb2+, Sr2+ and Zn2+ as well as lysophosphatidylcholine, lysophosphatidylethanolamine and p-bromophenacyl bromide (p-BPB) inhibited the enzyme strongly. The enzyme had an estimated molecular weight of 12,000 +/- 1,000 daltons on SDS-PAGE. Isoelectric focusing showed one PLA2 activity-containing band at pl 5.3. The purified enzyme hydrolysed linoleic acid at the sn-2 position of phosphatidylcholine and phosphatidylethanolamine with high selectivity, compared to arachidonic acid.
authors.affiliation: Department of Anatomy, University of Kuopio, Finland.
authors.forename: S
authors.initials: S
authors.lastname: Rönkkö
mesh_terms: D000818:Animals; D002417:Cattle; D008066:Lipolysis; D008297:Male; D010741:Phospholipases A / Q000302:isolation & purification* / Q000378:metabolism; D054467:Phospholipases A2; D011467:Prostate / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D010741:Phospholipases A; D054467:Phospholipases A2