抄録
1) Phospholipase A2 from aged frozen bovine pancreas was isolated and purified up to 299 folds by means of ion exchange Sephadex column chromatographr.
2) Bovine pancreatic phospholipase required special treatments to render the enzyme fully soluble in water.
3) Bovine phospholipase A2 was inhibited by EDTA and was made dependent on Ca++ ion. The optimum pH was around 8, and the optimum temperature showed a broad range between 25°-50°. However, pretreatment with an acidic medium at pH 3 at 90° for 5 min led to a high recovery of phospholipase A2 activity.
4) Leucine aminopeptidase containing a fraction obtained by ammonium sulfate fractionation appeared to inhibit the phospholipase activity thereafter.
5) The phospholipase A activity which appeared upon treatment with trypsin was likely to be prephospholipase.
