Purification of a Phospholipase A2 from Bungarus fasciatus Venom by One Step Sepharose 4B Method

By one step affinity chromatography (acid treated Sepharose 4B as matrix,tyrode solution containing 0.2 mol/L D-galactose as eluting solution),a phospholipase A2 was isolated from Bungarus fasciatus venom.Its partial N-terminal sequence is identical to previously reported Bungarus fasciatus venom phospholipase A2 isozyme Ⅵ (Lu & Lo,1978).This phospholipase A2 has only weak phospholipase A2 activity,no hemolytic nor hemorrhage activity.The enzyme exists as monomer and its molecular weight is 14 kDa,and has a relatively high carbohydrate content (13.4% w/w).