Studies on Phospholipase A2 from Bovine Pancreas
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概要
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1) Phospholipase A2 from aged frozen bovine pancreas was isolated and purified up to 299 folds by means of ion exchange Sephadex column chromatographr.<BR>2) Bovine pancreatic phospholipase required special treatments to render the enzyme fully soluble in water.<BR>3) Bovine phospholipase A2 was inhibited by EDTA and was made dependent on Ca<SUP>++</SUP> 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 A<SUB>2</SUB> activity.<BR>4) Leucine aminopeptidase containing a fraction obtained by ammonium sulfate fractionation appeared to inhibit the phospholipase activity thereafter.<BR>5) The phospholipase A activity which appeared upon treatment with trypsin was likely to be prephospholipase.
- Japan Society of Clinical Chemistryの論文
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