title: Purification and some properties of rat spleen phospholipase A2.
abstract: Intracellular phospholipase A2 was purified to homogeneity from rat spleen. The enzyme was efficiently concentrated by precipitation with trichloroacetic acid and purified by sequential use of column chromatographies on DEAE-Sepharose, octyl-Sepharose and Bio-Gel P-30. The positional specificity of the enzyme for an acylester bond at the sn-2-position of phospholipids was established. The purified enzyme has a pH optimum ranging from 8.0 to 10.5 and the molecular weight of the enzyme was estimated to be 14,700-14,800 by sodium dodecyl sulfate polyacrylamide gel electrophoresis and by gel filtration with a TSK-GEL G 2000 SW column. The purified enzyme requires Ca2+ for activity. The activity was not enhanced by the presence of purified calmodulin.
mesh_terms: D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002852:Chromatography, Ion Exchange; D008970:Molecular Weight; D010740:Phospholipases / Q000302:isolation & purification*; D010741:Phospholipases A / Q000302:isolation & purification*; D054467:Phospholipases A2; D051381:Rats; D013154:Spleen / Q000201:enzymology*
chemical_list: D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2; D002118:Calcium