Purification and Substrate Specificities of Phospholipase A and B of Sclerotinia Fungus
1963 年 27 巻 6 号 p. 397-404
詳細
1963 年 27 巻 6 号 p. 397-404
The phospholipase of Sclerotinia fungus was separated by the paperelectrophoresis method into three fractions, of which one component is phospholipase A and the others phospholipase B. These enzymes could be isolated also by the column chromatography using anion exchange resin Duolite A 2 and DEAE cellulose. The former and one of the latter enzymes were obtained in a crystalline form from its solution saturated with ammonium sulfate. The investigation of substrate specificities of these enzymes has shown that the two phospholipase B hydrolyze a commercial soybean lecithin, and one of them can also attack egg-yolk lecithin without addition of any activating lipides.
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